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Journal articles on the topic 'X-ray crystallography'

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Published: 4 June 2021
Last updated: 30 July 2024

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1

Bombicz, Petra. "X-ray crystallography." Crystallography Reviews 22, no. 1 (September 24, 2015): 79–81. http://dx.doi.org/10.1080/0889311x.2015.1082129.

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2

Wright, Jonathan. "X-ray crystallography." Crystallography Reviews 22, no. 4 (October 2016): 296–99. http://dx.doi.org/10.1080/0889311x.2016.1251424.

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3

Smyth, M. S. "x Ray crystallography." Molecular Pathology 53, no. 1 (February 1, 2000): 8–14. http://dx.doi.org/10.1136/mp.53.1.8.

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4

Helliwell, J. R. "X-ray crystallography." Physics Education 30, no. 6 (November 1995): 355–60. http://dx.doi.org/10.1088/0031-9120/30/6/007.

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5

Zou, Xiaodong, and Sven Hovmöller. "Electron crystallography: imaging and single-crystal diffraction from powders." Acta Crystallographica Section A Foundations of Crystallography 64, no. 1 (December 21, 2007): 149–60. http://dx.doi.org/10.1107/s0108767307060084.

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The study of crystals at atomic level by electrons – electron crystallography – is an important complement to X-ray crystallography. There are two main advantages of structure determinations by electron crystallography compared to X-ray diffraction: (i) crystals millions of times smaller than those needed for X-ray diffraction can be studied and (ii) the phases of the crystallographic structure factors, which are lost in X-ray diffraction, are present in transmission-electron-microscopy (TEM) images. In this paper, some recent developments of electron crystallography and its applications, mainly on inorganic crystals, are shown. Crystal structures can be solved to atomic resolution in two dimensions as well as in three dimensions from both TEM images and electron diffraction. Different techniques developed for electron crystallography, including three-dimensional reconstruction, the electron precession technique and ultrafast electron crystallography, are reviewed. Examples of electron-crystallography applications are given. There is in principle no limitation to the complexity of the structures that can be solved by electron crystallography.
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6

Nam, Ki-Hyun. "Approach of Serial Crystallography II." Crystals 11, no. 6 (June 9, 2021): 655. http://dx.doi.org/10.3390/cryst11060655.

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Serial crystallography (SX) is an emerging X-ray crystallographic method for determining macromolecule structures. It can address concerns regarding the limitations of data collected by conventional crystallography techniques, which require cryogenic-temperature environments and allow crystals to accumulate radiation damage. Time-resolved SX studies using the pump-probe methodology provide useful information for understanding macromolecular mechanisms and structure fluctuation dynamics. This Special Issue deals with the serial crystallography approach using an X-ray free electron laser (XFEL) and synchrotron X-ray source, and reviews recent SX research involving synchrotron use. These reports provide insights into future serial crystallography research trends and approaches.
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7

Nam, Ki. "Sample Delivery Media for Serial Crystallography." International Journal of Molecular Sciences 20, no. 5 (March 4, 2019): 1094. http://dx.doi.org/10.3390/ijms20051094.

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X-ray crystallographic methods can be used to visualize macromolecules at high resolution. This provides an understanding of molecular mechanisms and an insight into drug development and rational engineering of enzymes used in the industry. Although conventional synchrotron-based X-ray crystallography remains a powerful tool for understanding molecular function, it has experimental limitations, including radiation damage, cryogenic temperature, and static structural information. Serial femtosecond crystallography (SFX) using X-ray free electron laser (XFEL) and serial millisecond crystallography (SMX) using synchrotron X-ray have recently gained attention as research methods for visualizing macromolecules at room temperature without causing or reducing radiation damage, respectively. These techniques provide more biologically relevant structures than traditional X-ray crystallography at cryogenic temperatures using a single crystal. Serial femtosecond crystallography techniques visualize the dynamics of macromolecules through time-resolved experiments. In serial crystallography (SX), one of the most important aspects is the delivery of crystal samples efficiently, reliably, and continuously to an X-ray interaction point. A viscous delivery medium, such as a carrier matrix, dramatically reduces sample consumption, contributing to the success of SX experiments. This review discusses the preparation and criteria for the selection and development of a sample delivery medium and its application for SX.
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8

Nam, Ki Hyun. "Serial X-ray Crystallography." Crystals 12, no. 1 (January 13, 2022): 99. http://dx.doi.org/10.3390/cryst12010099.

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Serial crystallography (SX) is an emerging technique to determine macromolecules at room temperature. SX with a pump–probe experiment provides the time-resolved dynamics of target molecules. SX has developed rapidly over the past decade as a technique that not only provides room-temperature structures with biomolecules, but also has the ability to time-resolve their molecular dynamics. The serial femtosecond crystallography (SFX) technique using an X-ray free electron laser (XFEL) has now been extended to serial synchrotron crystallography (SSX) using synchrotron X-rays. The development of a variety of sample delivery techniques and data processing programs is currently accelerating SX research, thereby increasing the research scope. In this editorial, I briefly review some of the experimental techniques that have contributed to advances in the field of SX research and recent major research achievements. This Special Issue will contribute to the field of SX research.
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9

Rousse, Antoine, Christian Rischel, and Jean-Claude Gauthier. "Femtosecond x-ray crystallography." Reviews of Modern Physics 73, no. 1 (January 2, 2001): 17–31. http://dx.doi.org/10.1103/revmodphys.73.17.

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10

Romoli, Filippo, Estelle Mossou, Maxime Cuypers, Peter van der Linden, Philippe Carpentier, Sax A. Mason, V. Trevor Forsyth, and Sean McSweeney. "SPINE-compatible `carboloops': a new microshaped vitreous carbon sample mount for X-ray and neutron crystallography." Acta Crystallographica Section F Structural Biology Communications 70, no. 5 (April 15, 2014): 681–84. http://dx.doi.org/10.1107/s2053230x14005901.

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A novel vitreous carbon mount for macromolecular crystallography, suitable for neutron and X-ray crystallographic studies, has been developed. The technology described here is compatible both with X-ray and neutron cryo-crystallography. The mounts have low density and low background scattering for both neutrons and X-rays. They are prepared by laser cutting, allowing high standards of production quality, the ability to custom-design the mount to specific crystal sizes and large-scale production.
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11

Dodson, Guy. "Dorothy Mary Crowfoot Hodgkin, O.M. 12 May 1910 – 29 July 1994." Biographical Memoirs of Fellows of the Royal Society 48 (January 2002): 179–219. http://dx.doi.org/10.1098/rsbm.2002.0011.

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Dorothy Hodgkin was an X-ray crystallographer whose scientific career began in the 1930s and finished in the 1990s; her research had a deep influence on modern crystallography, chemistry and biochemistry. She had a profound grasp of crystallography and a genius for applying its methods. Her research was driven by the conviction that the X-ray image was the best basis for understanding the chemistry and function of molecules.
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12

Nazarenko, Alexander. "Crystallography Education for Non-Science College Students." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C1268. http://dx.doi.org/10.1107/s2053273314087312.

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New applications of crystallographic methods made it necessary to teach crystallography to students with limited background in physics and chemistry. In this case, classic approach to crystallography with mandatory study of space group and physics of X-ray diffraction is not feasible. We suggest an alternative direction: (1) introduction to experimental procedures and data collection for polycrystalline and (possibly) monocrystalline samples, (2) raw data processing and use of databases for identification of known crystalline materials. Instead of establishing a crystal structure of a new compound, our goal is limited to reliable identification of known one. With this approach, X-ray diffractometer appears to be one of many tools in analytical laboratory, and crystallographic data can be combined with results coming from multiple techniques such as Raman, IR, NMR, and mass-spectroscopy. Possible modifications of data collection and data processing procedures will be discussed. This presentation is based our experience with teaching various instrumental methods (including X-ray Crystallography) for Forensic and art conservation students at SUNY College at Buffalo.
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13

Wall, Michael E. "Quantum crystallographic charge density of urea." IUCrJ 3, no. 4 (June 8, 2016): 237–46. http://dx.doi.org/10.1107/s2052252516006242.

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Standard X-ray crystallography methods use free-atom models to calculate mean unit-cell charge densities. Real molecules, however, have shared charge that is not captured accurately using free-atom models. To address this limitation, a charge density model of crystalline urea was calculated using high-level quantum theory and was refined against publicly available ultra-high-resolution experimental Bragg data, including the effects of atomic displacement parameters. The resulting quantum crystallographic model was compared with models obtained using spherical atom or multipole methods. Despite using only the same number of free parameters as the spherical atom model, the agreement of the quantum model with the data is comparable to the multipole model. The static, theoretical crystalline charge density of the quantum model is distinct from the multipole model, indicating the quantum model provides substantially new information. Hydrogen thermal ellipsoids in the quantum model were very similar to those obtained using neutron crystallography, indicating that quantum crystallography can increase the accuracy of the X-ray crystallographic atomic displacement parameters. The results demonstrate the feasibility and benefits of integrating fully periodic quantum charge density calculations into ultra-high-resolution X-ray crystallographic model building and refinement.
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14

Dawe, Louise N. "Principles of X-ray crystallography." Crystallography Reviews 24, no. 1 (May 11, 2017): 65–67. http://dx.doi.org/10.1080/0889311x.2017.1320650.

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15

Spence, John C. H. "X-ray lasers and crystallography." IUCrJ 1, no. 3 (April 30, 2014): 151–52. http://dx.doi.org/10.1107/s2052252514009567.

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16

Ball, Philip. "X-Ray crystallography: Symmetry wars." Nature 492, no. 7427 (December 2012): 37–38. http://dx.doi.org/10.1038/492037a.

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17

Gerstner, Ed. "X-ray crystallography goes viral." Nature Physics 7, no. 3 (March 2011): 194. http://dx.doi.org/10.1038/nphys1950.

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18

Deschamps, Jeffrey R., and Clifford George. "Advances in X-ray crystallography." TrAC Trends in Analytical Chemistry 22, no. 8 (September 2003): 561–64. http://dx.doi.org/10.1016/s0165-9936(03)00902-6.

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19

Van Der Sluis, P., and J. Kroon. "Solvents and x-ray crystallography." Journal of Crystal Growth 97, no. 3-4 (October 1989): 645–56. http://dx.doi.org/10.1016/0022-0248(89)90566-6.

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20

Hauptman, Herbert A. "History of X-ray crystallography." Structural Chemistry 1, no. 6 (November 1990): 617–20. http://dx.doi.org/10.1007/bf00674136.

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21

Okada, Tetsuji, and Hitoshi Nakamichi. "X-ray crystallography of rhodopsin." Phase Transitions 77, no. 1-2 (January 2004): 21–29. http://dx.doi.org/10.1080/01411590310001621393.

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22

Hauptman, Herbert A. "History of X-ray crystallography." Chemometrics and Intelligent Laboratory Systems 10, no. 1-2 (February 1991): 13–18. http://dx.doi.org/10.1016/0169-7439(91)80029-p.

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23

Nam, Ki Hyun. "Serial X-ray Crystallography II." Crystals 13, no. 2 (January 25, 2023): 222. http://dx.doi.org/10.3390/cryst13020222.

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Traditional macromolecular crystallography (MX) and recently spotlighted cryogenic electron microscopy (Cryo-EM) techniques have contributed greatly to the development of macromolecule structures and the related fields [...]
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24

Kojić-Prodić, Biserka. "A century of X-ray crystallography and 2014 international year of X-ray crystallography." Macedonian Journal of Chemistry and Chemical Engineering 34, no. 1 (June 2, 2015): 19. http://dx.doi.org/10.20450/mjcce.2015.663.

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The 100<sup>th</sup> anniversary of the Nobel prize awarded to Max von Laue in 1914 for his discovery of diffraction of X-rays on a crystal marked the beginning of a new branch of science - X-ray crystallography. The experimental evidence of von Laue's discovery was given by physicists W. Friedrich and P. Knipping in 1912. In the same year W. L. Bragg described the analogy between X-rays and visible light and formulated the Bragg's law, a fundamental relation, that connected the wave nature of X-rays and fine structure of a crystal at atomic level. In 1913 the first simple diffractometer was constructed and structure determination started by the Braggs, father and son. In 1915 their discoveries were awarded by Nobel prize in physics. Since then, X-ray diffraction has been basic method for determination of three-dimensional structures of synthetic and natural compounds. The three-dimensional structure of molecule defines its physical, chemical, and biological properties. All over the past century significance of X-ray crystallography has been recognized by about forty Nobel prizes. The examples of X-ray structure analysis, of simple crystals of rock salt, diamond and graphite, and then of complex biomolecules such as B12-vitamin, penicillin, haemoglobin/myoglobin, DNA, and biomolecular complexes such as viruses, chromatin, ribozyme, and other molecular machines, have illustrated the development of the method. Among these big discoveries double helix DNA structure is epochal one of 20<sup>th</sup> century. These discoveries together with many others within X-ray crystallography completely changed our views and helped to be developed different new fields of science such as molecular genetics, biophysics, structural molecular biology, material science, and many others. During the last decade, an implementation of free electron X-ray lasers, a new experimental tool, has opened up femtosecond dynamic crystallography. This highly advanced methodology enables to solve the structures and dynamics of the most complex biological assemblies involved in a cell metabolism. The advancements of science and technology over 20<sup>th</sup> and 21<sup>st</sup>centuries are of great influence on our views in almost all human activities. The importance of X-ray crystallography for science and technology advocates for its high impact on a wide area of research and declares it as highly interdisciplinary science. Briefly saying, crystallography defines the shape of our modern world.<p>The essay is far from being complete and it is concentrated on single crystal diffraction. The wide area of X-ray crystallography hardly can be reviewed in a single article. However, it highlights the most striking examples illustrating some of the milestones over past century.</p><p> </p>
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25

Downing, Kenneth H., and Huilin Li. "Accurate Recording and Measurement of Electron Diffraction Data in Structural and Difference Fourier Studies of Proteins." Microscopy and Microanalysis 7, no. 5 (September 2001): 407–17. http://dx.doi.org/10.1007/s10005-001-0014-2.

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AbstractMany of the techniques that have been developed in X-ray crystallography are being applied in electron crystallographic studies of proteins. Electron crystallography has the advantage of measuring structure factor phases directly from high resolution images with an accuracy substantially higher than is common in X-ray crystallography. However, electron diffraction amplitudes are often not as precise as those obtained in X-ray work. We discuss here some approaches to maximizing the reliability of the diffraction amplitudes through choice of exposure and data processing schemes. With accurate measurement of diffraction data, Fourier difference methods can be used in electron crystallographic studies of small, localized changes of proteins that exist in two-dimensional crystals. The mathematical basis for the power of these methods in detecting small changes is reviewed. We then discuss several issues related to optimizing the quality of the diffraction data and derive an expression for the best exposure for recording diffraction patterns. An application of Fourier difference maps in localizing drug binding sites on the protein tubulin is discussed.
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26

Zeng, Lingxiao, Wei Ding, and Quan Hao. "Using cryo-electron microscopy maps for X-ray structure determination." IUCrJ 5, no. 4 (May 11, 2018): 382–89. http://dx.doi.org/10.1107/s2052252518005857.

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X-ray crystallography and cryo-electron microscopy (cryo-EM) are complementary techniques for structure determination. Crystallography usually reveals more detailed information, while cryo-EM is an extremely useful technique for studying large-sized macromolecules. As the gap between the resolution of crystallography and cryo-EM data narrows, the cryo-EM map of a macromolecule could serve as an initial model to solve the phase problem of crystal diffraction for high-resolution structure determination. FSEARCH is a procedure to utilize the low-resolution molecular shape for crystallographic phasing. The IPCAS (Iterative Protein Crystal structure Automatic Solution) pipeline is an automatic direct-methods-aided dual-space iterative phasing and model-building procedure. When only an electron-density map is available as the starting point, IPCAS is capable of generating a completed model from the phases of the input map automatically, without the requirement of an initial model. In this study, a hybrid method integrating X-ray crystallography with cryo-EM to help with structure determination is presented. With a cryo-EM map as the starting point, the workflow of the method involves three steps. (1) Cryo-EM map replacement: FSEARCH is utilized to find the correct translation and orientation of the cryo-EM map in the crystallographic unit cell and generates the initial low-resolution map. (2) Phase extension: the phases calculated from the correctly placed cryo-EM map are extended to high-resolution X-ray data by non-crystallographic symmetry averaging with phenix.resolve. (3) Model building: IPCAS is used to generate an initial model using the phase-extended map and perform model completion by iteration. Four cases (the lowest cryo-EM map resolution being 6.9 Å) have been tested for the general applicability of the hybrid method, and almost complete models have been generated for all test cases with reasonable R work/R free. The hybrid method therefore provides an automated tool for X-ray structure determination using a cryo-EM map as the starting point.
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27

Stewart, P. L., S. D. Fuller, and R. M. Burnett. "Bridging the resolution gap between x-ray crystallography and electron microscopy." Proceedings, annual meeting, Electron Microscopy Society of America 52 (1994): 92–93. http://dx.doi.org/10.1017/s0424820100168190.

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While x-ray crystallography provides atomic resolution structures of proteins and small viruses, electron microscopy can provide complementary structural information on larger assemblies. A significant computational challenge is faced in bridging the resolution gap between the two techniques. X-ray crystallographic data is collected in the range of 2-10 Å, while image reconstructions from electron micrographs are at a resolution of 25-35 Å. A further problem is that density derived from cryo-electron micrographs is distorted by the contrast transfer function of the microscope, whichaccentuates certain resolution bands.A novel combination of electron microscopy and x-ray crystallography has revealed the various structural components forming the capsid of human type 2 adenovirus. An image reconstruction of the intact virus (Fig. 1), derived from cryo-electron micrographs, was deconvolved with an approximate contrast transfer function to mitigate microscope distortions (Fig. 2). A model capsid was calculated from 240 copies of the crystallographic structure of the major capsid protein and filtered to the correct resolution (Fig. 3).
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28

Arndt, U. W. "Instrumentation in X-ray crystallography: Past, present and future." Notes and Records of the Royal Society of London 55, no. 3 (September 22, 2001): 457–72. http://dx.doi.org/10.1098/rsnr.2001.0157.

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This paper deals with the very great changes in X–ray crystallographic techniques and apparatus over a period of approximately the last 60 years. This is not a general history; it is a personal account of the developments with which I have been directly involved; it is, therefore, biased towards apparatus developments in the field of macromolecular crystallography in which I have worked during most of this period. The bias needs little excuse: many of the new techniques of X–ray crystallography were devised initially for large–molecule structure determinations which had most need of such advances in order to be feasible at all. Among them are the uses of computers in calculating electron density maps, the construction of automatic diffractometers and microdensitometers, the introduction of rotating-anode X–ray generators and of microfocus X–ray tubes, the development of electronic X–ray area detectors, the pioneering work on the use of synchrotron radiation for diffraction studies, the building of three–dimensional atomic models by computer and the complete automation of the mounting, selection and alignment of crystals on the diffractometer.
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29

Bernhardt, Paul V., Raymond M. Carman, and Tri T. Le. "The Stereo Structures of Some Mycophenolic Acid Derivatives." Australian Journal of Chemistry 60, no. 5 (2007): 354. http://dx.doi.org/10.1071/ch06481.

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30

Gevorkov, Yaroslav, Anton Barty, Wolfgang Brehm, Thomas A. White, Aleksandra Tolstikova, Max O. Wiedorn, Alke Meents, Rolf-Rainer Grigat, Henry N. Chapman, and Oleksandr Yefanov. "pinkIndexer – a universal indexer for pink-beam X-ray and electron diffraction snapshots." Acta Crystallographica Section A Foundations and Advances 76, no. 2 (January 10, 2020): 121–31. http://dx.doi.org/10.1107/s2053273319015559.

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A crystallographic indexing algorithm, pinkIndexer, is presented for the analysis of snapshot diffraction patterns. It can be used in a variety of contexts including measurements made with a monochromatic radiation source, a polychromatic source or with radiation of very short wavelength. As such, the algorithm is particularly suited to automated data processing for two emerging measurement techniques for macromolecular structure determination: serial pink-beam X-ray crystallography and serial electron crystallography, which until now lacked reliable programs for analyzing many individual diffraction patterns from crystals of uncorrelated orientation. The algorithm requires approximate knowledge of the unit-cell parameters of the crystal, but not the wavelengths associated with each Bragg spot. The use of pinkIndexer is demonstrated by obtaining 1005 lattices from a published pink-beam serial crystallography data set that had previously yielded 140 indexed lattices. Additionally, in tests on experimental serial crystallography diffraction data recorded with quasi-monochromatic X-rays and with electrons the algorithm indexed more patterns than other programs tested.
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31

Pinkerton, A. Alan. "Why crystal structure analysis works: a one-dimensional crystallography teaching tool." Journal of Applied Crystallography 48, no. 3 (May 22, 2015): 901–5. http://dx.doi.org/10.1107/s1600576715007116.

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A teaching tool is proposed to help beginner students of crystallography understand how crystallographic calculations work. Examples of the most important methods taught in X-ray crystallography courses have been adapted to a one-dimensional hypothetical structure. All calculations can be carried out in class with a scientific calculator or by using a simple spreadsheet.
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32

Hutchison, Christopher D. M., and Jasper J. van Thor. "Optical control, selection and analysis of population dynamics in ultrafast protein X-ray crystallography." Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences 377, no. 2145 (April 2019): 20170474. http://dx.doi.org/10.1098/rsta.2017.0474.

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Ultrafast pump-probe X-ray crystallography has now been established at X-ray free electron lasers that operate at hard X-ray energies. We discuss the performance and development of current applications in terms of the available data quality and sensitivity to detect and analyse structural dynamics. A discussion of technical capabilities expected at future high repetition rate applications as well as future non-collinear multi-pulse schemes focuses on the possibility to advance the technique to the practical application of the X-ray crystallographic equivalent of an impulse time-domain Raman measurement of vibrational coherence. Furthermore, we present calculations of the magnitude of population differences and distributions prepared with ultrafast optical pumping of single crystals in the typical serial femtosecond crystallography geometry, which are developed for the general uniaxial and biaxial cases. The results present opportunities for polarization resolved anisotropic X-ray diffraction analysis of photochemical populations for the ultrafast time domain. This article is part of the theme issue ‘Measurement of ultrafast electronic and structural dynamics with X-rays’.
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33

Iqra Zubair Awan, Iqra Zubair Awan. "X-Ray Diffraction – The Magic Wand." Journal of the chemical society of pakistan 42, no. 3 (2020): 317. http://dx.doi.org/10.52568/000646.

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This review paper covers one of the most important discoveries of the last century, viz. X-ray diffraction. It has made enormous contribution to chemistry, physics, engineering, materials science, crystallography and above all medical sciences. The review covers the history of X-rays detection and production, its uses/ applications. The scientific and medical community will forever be indebted to Rand#246;ntgen for this invaluable discovery and to those who perfected its application.
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34

Iqra Zubair Awan, Iqra Zubair Awan. "X-Ray Diffraction – The Magic Wand." Journal of the chemical society of pakistan 42, no. 3 (2020): 317. http://dx.doi.org/10.52568/000646/jcsp/42.03.2020.

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This review paper covers one of the most important discoveries of the last century, viz. X-ray diffraction. It has made enormous contribution to chemistry, physics, engineering, materials science, crystallography and above all medical sciences. The review covers the history of X-rays detection and production, its uses/ applications. The scientific and medical community will forever be indebted to Rand#246;ntgen for this invaluable discovery and to those who perfected its application.
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35

McPherson, Alexander. "In situX-ray crystallography." Journal of Applied Crystallography 33, no. 2 (April 1, 2000): 397–400. http://dx.doi.org/10.1107/s0021889800001254.

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A method is proposed, and preliminary experiments are described, for collection of X-ray data from macromolecular crystalsin situ. The usual processes of mounting for either room-temperature or cryogenic X-ray data collection are eliminated by growing crystals, using vapor diffusion, on small supports or films that can be either frozen or treated before transfer directly to the X-ray beam. The approach has the advantage that individual crystals are never manipulated and it is not necessary to isolate single crystals. Furthermore, crystals fixed to the surface on which they grow provides a positive advantage, small and otherwise problematic crystals become serviceable, and robotic or automated data collection becomes simplified.
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36

Weik, Martin, and Jacques-Philippe Colletier. "Temperature-dependent macromolecular X-ray crystallography." Acta Crystallographica Section D Biological Crystallography 66, no. 4 (March 24, 2010): 437–46. http://dx.doi.org/10.1107/s0907444910002702.

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X-ray crystallography provides structural details of biological macromolecules. Whereas routine data are collected close to 100 K in order to mitigate radiation damage, more exotic temperature-controlled experiments in a broader temperature range from 15 K to room temperature can provide both dynamical and structural insights. Here, the dynamical behaviour of crystalline macromolecules and their surrounding solvent as a function of cryo-temperature is reviewed. Experimental strategies of kinetic crystallography are discussed that have allowed the generation and trapping of macromolecular intermediate states by combining reaction initiation in the crystalline state with appropriate temperature profiles. A particular focus is on recruiting X-ray-induced changes for reaction initiation, thus unveiling useful aspects of radiation damage, which otherwise has to be minimized in macromolecular crystallography.
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37

Horrell, Sam, Svetlana V. Antonyuk, Robert R. Eady, S. Samar Hasnain, Michael A. Hough, and Richard W. Strange. "Serial crystallography captures enzyme catalysis in copper nitrite reductase at atomic resolution from one crystal." IUCrJ 3, no. 4 (June 15, 2016): 271–81. http://dx.doi.org/10.1107/s205225251600823x.

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Relating individual protein crystal structures to an enzyme mechanism remains a major and challenging goal for structural biology. Serial crystallography using multiple crystals has recently been reported in both synchrotron-radiation and X-ray free-electron laser experiments. In this work, serial crystallography was used to obtain multiple structures serially from one crystal (MSOX) to studyin crystalloenzyme catalysis. Rapid, shutterless X-ray detector technology on a synchrotron MX beamline was exploited to perform low-dose serial crystallography on a single copper nitrite reductase crystal, which survived long enough for 45 consecutive 100 K X-ray structures to be collected at 1.07–1.62 Å resolution, all sampled from the same crystal volume. This serial crystallography approach revealed the gradual conversion of the substrate bound at the catalytic type 2 Cu centre from nitrite to nitric oxide, following reduction of the type 1 Cu electron-transfer centre by X-ray-generated solvated electrons. Significant, well defined structural rearrangements in the active site are evident in the series as the enzyme moves through its catalytic cycle, namely nitrite reduction, which is a vital step in the global denitrification process. It is proposed that such a serial crystallography approach is widely applicable for studying any redox or electron-driven enzyme reactions from a single protein crystal. It can provide a `catalytic reaction movie' highlighting the structural changes that occur during enzyme catalysis. The anticipated developments in the automation of data analysis and modelling are likely to allow seamless and near-real-time analysis of such data on-site at some of the powerful synchrotron crystallographic beamlines.
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38

KIM, Chae Un. "High-Pressure X-ray Protein Crystallography." Physics and High Technology 24, no. 9 (September 30, 2015): 19. http://dx.doi.org/10.3938/phit.24.044.

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39

Brewster, Aaron, and Herbert Bernstein. "Metadata standards in X-ray crystallography." Acta Crystallographica Section A Foundations and Advances 78, a1 (July 29, 2022): a126. http://dx.doi.org/10.1107/s2053273322098734.

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40

TSUKIHARA, Tomitake. "X-Ray crystallography in structural biology." Seibutsu Butsuri 36, no. 5 (1996): 211–15. http://dx.doi.org/10.2142/biophys.36.211.

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41

YASUOKA, Noritake. "Computer graphics in X-ray crystallography." Nihon Kessho Gakkaishi 29, no. 1 (1987): 57–63. http://dx.doi.org/10.5940/jcrsj.29.57.

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42

Ki, Hosung, Key Young Oang, Jeongho Kim, and Hyotcherl Ihee. "Ultrafast X-Ray Crystallography and Liquidography." Annual Review of Physical Chemistry 68, no. 1 (May 5, 2017): 473–97. http://dx.doi.org/10.1146/annurev-physchem-052516-050851.

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43

Kemp, Terence J., and Nathaniel W. Alcock. "100 Years of X-ray Crystallography." Science Progress 100, no. 1 (March 2017): 25–44. http://dx.doi.org/10.3184/003685017x14858694684395.

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The developments in crystallography, since it was first covered in Science Progress in 1917, following the formulation of the Bragg equation, are described. The advances in instrumentation and data analysis, coupled with the application of computational methods to data analysis, have enabled the solution of molecular structures from the simplest binary systems to the most complex of biological structures. These developments are shown to have had major impacts in the development of chemical bonding theory and in offering an increasing understanding of enzyme–substrate interactions. The advent of synchrotron radiation sources has opened a new chapter in this multi-disciplinary field of science.
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44

Schwarzenbach, Dieter. "Early days of x-ray crystallography." Crystallography Reviews 20, no. 2 (January 10, 2014): 155–56. http://dx.doi.org/10.1080/0889311x.2013.876419.

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45

Spence, John C. H. "X-ray lasers and serial crystallography." IUCrJ 2, no. 3 (April 30, 2015): 305–6. http://dx.doi.org/10.1107/s2052252515008027.

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46

Singh, Appu K., Luke L. McGoldrick, Kei Saotome, and Alexander I. Sobolevsky. "X-ray crystallography of TRP channels." Channels 12, no. 1 (January 1, 2018): 137–52. http://dx.doi.org/10.1080/19336950.2018.1457898.

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47

Yaffe, Michael B. "X-ray crystallography and structural biology." Critical Care Medicine 33, Suppl (December 2005): S435—S440. http://dx.doi.org/10.1097/01.ccm.0000191719.66383.01.

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48

Delpierre, P., J. F. Berar, L. Blanquart, B. Caillot, J. C. Clemens, and C. Mouget. "X-ray pixel detector for crystallography." IEEE Transactions on Nuclear Science 48, no. 4 (2001): 987–91. http://dx.doi.org/10.1109/23.958710.

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49

Thomas, John Meurig. "The birth of X-ray crystallography." Nature 491, no. 7423 (November 2012): 186–87. http://dx.doi.org/10.1038/491186a.

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50

Deschamps, Jeffrey R. "X-ray crystallography of chemical compounds." Life Sciences 86, no. 15-16 (April 2010): 585–89. http://dx.doi.org/10.1016/j.lfs.2009.02.028.

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