Processing of X-ray snapshots from crystals in random orientations

Autor: Wolfgang Kabsch

Publikováno v: Acta Crystallographica Section D: Biological Crystallography

A new method for the treatment of partial reflections from X-ray snapshots is implemented in the program package nXDS, which yields intensity data of almost the same quality as those obtained by the classical rotation method.
A functional expres

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::894a97c79029f5321d1d14560e0109c5
https://doi.org/10.1107/s1399004714013534

A New View of the Mechanisms of UDP-N-Acetylglucosamine Enolpyruvyl Transferase (MurA) and 5-Enolpyruvylshikimate-3-phosphate Synthase (AroA) Derived from X-ray Structures of Their Tetrahedral Reaction Intermediate States

Autor: Ernst Schönbrunn, M.L. Healy, Susanne Eschenburg, Wolfgang Kabsch

Publikováno v: Journal of Biological Chemistry. 278:49215-49222

UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) and 5-enolpyruvylshikimate-3-phosphate synthase (AroA) constitute the small enzyme family of enolpyruvyl transferases, which catalyze the chemically unusual reaction of enolpyruvyl transfer. MurA

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4f8e2adcdd80fb9b6cd4906e0175e2b
https://doi.org/10.1074/jbc.m309741200

Indications of radiation damage in ferredoxin microcrystals using high-intensity X-FEL beams

Autor: Thomas R. M. Barends, Garth J. Williams, Wolfgang Kabsch, Jonas Lindholt Gregersen, Daniel Mattle, Poul Nissen, Roberto Alonso-Mori, Stefan P. Hau-Riege, Saša Bajt, H. Olof Jönsson, Carl Caleman, Jason E. Koglin, Sébastien Boutet, Nikolaj D. Drachmann, Sabine Botha, Stephan Kassemeyer, Oleg Sitsel, Ilme Schlichting, Michael Krumrey, Marc Messerschmidt, Henry N. Chapman, Kenneth R. Beyerlein, Lutz Foucar, Anton Barty, Nicusor Timneanu, Dimosthenis Sokaras, Elisabeth Hartmann, Karol Nass, Andrew Aquila, Maike Bublitz, R. Bruce Doak, Richard Bean, Robert L. Shoeman, Linda Reinhard

Publikováno v: Nass, K, Foucar, L, Barends, T R M, Hartmann, E, Botha, S, Shoeman, R L, Doak, R B, Alonso-Mori, R, Aquila, A, Bajt, S, Barty, A, Bean, R, Beyerlein, K R, Bublitz, M, Drachmann, N, Gregersen, J, Jönsson, H O, Kabsch, W, Kassemeyer, S, Koglin, J E, Krumrey, M, Mattle, D, Messerschmidt, M, Nissen, P, Reinhard (maiden name Schuldt), L, Sitsel, O, Sokaras, D, Williams, G J, Hau-Riege, S, Timneanu, N, Caleman, C, Chapman, H N, Boutet, S & Schlichting, I 2015, ' Indications of radiation damage in ferredoxin microcrystals using high-intensity X-FEL beams ', Journal of Synchrotron Radiation, vol. 22, no. 2, pp. 225-238 . https://doi.org/10.1107/S1600577515002349
Journal of Synchrotron Radiation
Journal of synchrotron radiation 22(2), 225-238 (2015). doi:10.1107/S1600577515002349

Proteins that contain metal cofactors are expected to be highly radiation sensitive since the degree of X-ray absorption correlates with the presence of high-atomic-number elements and X-ray energy. To explore the effects of local damage in serial fe

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4dca1faabfc67f555f9bbbbe0b80f52b
https://pubmed.ncbi.nlm.nih.gov/25723924

[Untitled]

Autor: A. F. Volker Wagner, Karin Fritz-Wolf, Joachim Knappe, S. Schultz, Andreas Becker, Wolfgang Kabsch

Publikováno v: Nature Structural Biology. 6:969-975

Pyruvate formate-lyase (PFL) from Escherichia coli uses a radical mechanism to reversibly cleave the C1-C2 bond of pyruvate using the Gly 734 radical and two cysteine residues (Cys 418, Cys 419). We have determined by X-ray crystallography the struct

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::cc4880e4fb6e9cc09b52eaa0c3dd82e3
https://doi.org/10.1038/13341

The Ras-RasGAP Complex: How to Complement an Inefficient Active Site

Autor: Mohammad Reza Ahmadian, Alfred Wittinghofer, Klaus Scheffzek, Wolfgang Kabsch, Lisa Wiesmüller, Frank Schmitz, Alfred Lautwein

Publikováno v: Phosphorus, Sulfur, and Silicon and the Related Elements. 144:741-744

GTP-hydrolysis as carried out by GTP-binding proteins[1] is intrinsically very slow but can be accelerated by orders of magnitude upon interaction with GTPase Activating Proteins, GAPs, which are specific for the respective GTP-binding proteins. Focu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::dca0d71aece0cdb2a628690e24116158
https://doi.org/10.1080/10426509908546351