Works matching X-ray crystallography

Results: 5000
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    Beamline X29: a novel undulator source for X-ray crystallography.

    Published in:
    2006
    By:
    • Shi, Wuxian;
    • Robinson, Howard;
    • Sullivan, Michael;
    • Abel, Don;
    • Toomey, John;
    • Berman, Lonny E.;
    • Lynch, Don;
    • Rosenbaum, Gerd;
    • Rakowsky, George;
    • Rock, Larry;
    • Nolan, Bill;
    • Shea-McCarthy, Grace;
    • Schneider, Dieter;
    • Johnson, Erik;
    • Sweet, Robert M.;
    • Chance, Mark R.
    Publication type:
    Other
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    Serial X-ray Crystallography.

    Published in:
    Crystals (2073-4352), 2022, v. 12, n. 1, p. 99, doi. 10.3390/cryst12010099
    By:
    • Nam, Ki Hyun
    Publication type:
    Article
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    Why do we trust X-ray crystallography?

    Published in:
    Resonance: Journal of Science Education, 2014, v. 19, n. 12, p. 1087, doi. 10.1007/s12045-014-0134-7
    By:
    • Bond, Andrew
    Publication type:
    Article
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    "Seeing Is Believing": How Neutron Crystallography Informs Enzyme Mechanisms by Visualizing Unique Water Species hydrogen is the lightest atom and composes approximately half of the atomic content in macromolecules, yet their location can only be inferred or predicted in most macromolecular structures. This is because hydrogen can rarely be directly observed by the most common structure determination techniques (such as X-ray crystallography and electron cryomicroscopy). However, knowledge of hydrogen atom positions, especially for enzymes, can reveal protonation states of titratable active site residues, hydrogen bonding patterns, and the orientation of water molecules. Though we know they are present, this vital layer of information, which can inform a myriad of biological processes, is frustratingly invisible to us. The good news is that, even at modest resolution, neutron crystallography (NC) can reveal this layer and has emerged this century as a powerful tool to elucidate enzyme catalytic mechanisms. Due to its strong and coherent scattering of neutrons, incorporation of deuterium into the protein crystal amplifies the power of NC. This is especially true when solvation and the specific participation of key water molecules are crucial for catalysis. Neutron data allow the modeling of all three atoms in water molecules and have even revealed previously unobserved and unique species such as hydronium (D<sub>3</sub>O<sup>+</sup>) and deuteroxide (OD<sup>−</sup>) ions as well as lone deuterons (D<sup>+</sup>). Herein, we briefly review why neutrons are ideal probes for identifying catalytically important water molecules and these unique water-like species, limitations in interpretation, and four vignettes of enzyme success stories from disparate research groups. One of these groups was that of Dr. Chris G. Dealwis, who died unexpectedly in 2022. As a memorial appreciation of his scientific career, we will also highlight his interest and contributions to the

    Published in:
    Biology (2079-7737), 2024, v. 13, n. 11, p. 850, doi. 10.3390/biology13110850
    By:
    • Wan, Qun;
    • Bennett, Brad C.
    Publication type:
    Article
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    Insight into small molecule binding to the neonatal Fc receptor by X-ray crystallography and 100 kHz magic-angle-spinning NMR.

    Published in:
    PLoS Biology, 2018, v. 16, n. 5, p. 1, doi. 10.1371/journal.pbio.2006192
    By:
    • Stöppler, Daniel;
    • Macpherson, Alex;
    • Smith-Penzel, Susanne;
    • Basse, Nicolas;
    • Lecomte, Fabien;
    • Deboves, Hervé;
    • Taylor, Richard D.;
    • Norman, Tim;
    • Porter, John;
    • Waters, Lorna C.;
    • Westwood, Marta;
    • Cossins, Ben;
    • Cain, Katharine;
    • White, James;
    • Griffin, Robert;
    • Prosser, Christine;
    • Kelm, Sebastian;
    • Sullivan, Amy H.;
    • IIIFox, David;
    • Carr, Mark D.
    Publication type:
    Article
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