The Experts below are selected from a list of 129924 Experts worldwide ranked by ideXlab platform
Jean François Guichou - One of the best experts on this subject based on the ideXlab platform.
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Combining 'dry' co-crystallization and in situ diffraction to facilitate ligand screening by X-Ray Crystallography.
Acta Crystallographica Section D: Biological Crystallography, 2015Co-Authors: Muriel Gelin, Vanessa Delfosse, Frédéric Allemand, François Hoh, Yoann Sallaz-damaz, Michel Pirocchi, William Bourguet, Jean-luc Ferrer, Gilles Labesse, Jean François GuichouAbstract:X-Ray Crystallography is an established technique for ligand screening in fragment-based drug-design projects, but the required manual handling steps - soaking crystals with ligand and the subsequent harvesting - are tedious and limit the throughput of the process. Here, an alternative approach is reported: crystallization plates are pre-coated with potential binders prior to protein crystallization and X-Ray diffraction is performed directly 'in situ' (or in-plate). Its performance is demonstrated on distinct and relevant therapeutic targets currently being studied for ligand screening by X-Ray Crystallography using either a bending-magnet beamline or a rotating-anode generator. The possibility of using DMSO stock solutions of the ligands to be coated opens up a route to screening most chemical libraries.
Jiawei Wang - One of the best experts on this subject based on the ideXlab platform.
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how cryo electron microscopy and X Ray Crystallography complement each other
Protein Science, 2017Co-Authors: Hongwei Wang, Jiawei WangAbstract:With the ability to resolve structures of macromolecules at atomic resolution, X-Ray Crystallography has been the most powerful tool in modern structural biology. At the same time, recent technical improvements have triggered a resolution revolution in the single particle cryo-EM method. While the two methods are different in many respects, from sample preparation to structure determination, they both have the power to solve macromolecular structures at atomic resolution. It is important to understand the unique advantages and caveats of the two methods in solving structures and to appreciate the complementary nature of the two methods in structural biology. In this review we provide some eXamples, and discuss how X-Ray Crystallography and cryo-EM can be combined in deciphering structures of macromolecules for our full understanding of their biological mechanisms.
Muriel Gelin - One of the best experts on this subject based on the ideXlab platform.
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Combining 'dry' co-crystallization and in situ diffraction to facilitate ligand screening by X-Ray Crystallography.
Acta Crystallographica Section D: Biological Crystallography, 2015Co-Authors: Muriel Gelin, Vanessa Delfosse, Frédéric Allemand, François Hoh, Yoann Sallaz-damaz, Michel Pirocchi, William Bourguet, Jean-luc Ferrer, Gilles Labesse, Jean François GuichouAbstract:X-Ray Crystallography is an established technique for ligand screening in fragment-based drug-design projects, but the required manual handling steps - soaking crystals with ligand and the subsequent harvesting - are tedious and limit the throughput of the process. Here, an alternative approach is reported: crystallization plates are pre-coated with potential binders prior to protein crystallization and X-Ray diffraction is performed directly 'in situ' (or in-plate). Its performance is demonstrated on distinct and relevant therapeutic targets currently being studied for ligand screening by X-Ray Crystallography using either a bending-magnet beamline or a rotating-anode generator. The possibility of using DMSO stock solutions of the ligands to be coated opens up a route to screening most chemical libraries.
Hongwei Wang - One of the best experts on this subject based on the ideXlab platform.
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how cryo electron microscopy and X Ray Crystallography complement each other
Protein Science, 2017Co-Authors: Hongwei Wang, Jiawei WangAbstract:With the ability to resolve structures of macromolecules at atomic resolution, X-Ray Crystallography has been the most powerful tool in modern structural biology. At the same time, recent technical improvements have triggered a resolution revolution in the single particle cryo-EM method. While the two methods are different in many respects, from sample preparation to structure determination, they both have the power to solve macromolecular structures at atomic resolution. It is important to understand the unique advantages and caveats of the two methods in solving structures and to appreciate the complementary nature of the two methods in structural biology. In this review we provide some eXamples, and discuss how X-Ray Crystallography and cryo-EM can be combined in deciphering structures of macromolecules for our full understanding of their biological mechanisms.
Axel T. Brunger - One of the best experts on this subject based on the ideXlab platform.
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X-Ray Crystallography and NMR reveal complementary views of structure and dynamics.
Nature Structural & Molecular Biology, 1997Co-Authors: Axel T. BrungerAbstract:X-Ray Crystallography and nuclear magnetic resonance spectroscopy are not competing techniques, but rather they complement each other. Taken together they can provide an atomic detail picture of macromolecular structure and dynamics which can be used to obtain an understanding of life processes at the molecular level.
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Computational challenges for macromolecular structure determination by X-Ray Crystallography and solution NMRspectroscopy
Quarterly Reviews of Biophysics, 1993Co-Authors: Axel T. Brunger, Michael NilgesAbstract:Macromolecular structure determination by X-Ray Crystallography and solution NMR spectroscopy has eXperienced unprecedented growth during the past decade.