Combining on-line spectroscopy with synchrotron and X-ray free electron laser crystallography |
| |
| Institution: | 1. ESRF - The European Synchrotron, 71 Avenue des Martyrs, CS40220, 38043 Grenoble Cedex 9, France;2. Univ. Grenoble Alpes, CNRS, CEA, IBS, F-38000 Grenoble, France;1. Department of Chemistry and Chemical Biology and Center for Biotechnology and Interdisciplinary Sciences, Rensselaer Polytechnic Institute, Troy, NY, 12180, USA;2. Institute for Protein Design, University of Washington, Seattle, WA, 98195, USA;3. Department of Medicinal Chemistry, University of Washington, Seattle, WA, 98195, USA;1. Magnetic Resonance Center (CERM), University of Florence, Via Sacconi 6, Sesto Fiorentino, 50019, Italy;2. Department of Chemistry “Ugo Schiff”, University of Florence, Via della Lastruccia 3, Sesto Fiorentino, 50019, Italy;3. Consorzio Interuniversitario Risonanze Magnetiche Metallo Proteine (CIRMMP), Via Sacconi 6, Sesto Fiorentino, 50019, Italy;1. State Key Laboratory of Membrane Biology, Beijing Frontier Research Center for Biological Structure, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China;2. School of Life Sciences, Cryo-EM Center, Southern University of Science and Technology, Shenzhen 518055, Guangdong, China;1. Technische Universität Berlin, Chair of Bioanalytics, 10623 Berlin, Germany;2. Si-M/“Der Simulierte Mensch”, a Science Framework of Technische Universität Berlin and Charité - Universitätsmedizin Berlin, 10623 Berlin, Germany;3. Wellcome Centre for Cell Biology, University of Edinburgh, Edinburgh EH9 3BF, UK |
| |
| Abstract: | With the recent advances in serial crystallography methods at both synchrotron and X-ray free electron laser sources, more details of intermediate or transient states of the catalytic reactions are being revealed structurally. These structural studies of reaction dynamics drive the need for on-line in crystallo spectroscopy methods to complement the crystallography experiment. The recent applications of combined spectroscopy and crystallography methods enable on-line determination of in crystallo reaction kinetics and structures of catalytic intermediates, sample integrity, and radiation-induced sample modifications, if any, as well as heterogeneity of crystals from different preparations or sample batches. This review describes different modes of spectroscopy that are combined with the crystallography experiment at both synchrotron and X-ray free-electron laser facilities, and the complementary information that each method can provide to facilitate the structural study of enzyme catalysis and protein dynamics. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
