| Literature DB >> 22286384 |
Rudolf Koopmann1, Karolina Cupelli, Lars Redecke, Karol Nass, Daniel P Deponte, Thomas A White, Francesco Stellato, Dirk Rehders, Mengning Liang, Jakob Andreasson, Andrew Aquila, Sasa Bajt, Miriam Barthelmess, Anton Barty, Michael J Bogan, Christoph Bostedt, Sébastien Boutet, John D Bozek, Carl Caleman, Nicola Coppola, Jan Davidsson, R Bruce Doak, Tomas Ekeberg, Sascha W Epp, Benjamin Erk, Holger Fleckenstein, Lutz Foucar, Heinz Graafsma, Lars Gumprecht, Janos Hajdu, Christina Y Hampton, Andreas Hartmann, Robert Hartmann, Günter Hauser, Helmut Hirsemann, Peter Holl, Mark S Hunter, Stephan Kassemeyer, Richard A Kirian, Lukas Lomb, Filipe R N C Maia, Nils Kimmel, Andrew V Martin, Marc Messerschmidt, Christian Reich, Daniel Rolles, Benedikt Rudek, Artem Rudenko, Ilme Schlichting, Joachim Schulz, M Marvin Seibert, Robert L Shoeman, Raymond G Sierra, Heike Soltau, Stephan Stern, Lothar Strüder, Nicusor Timneanu, Joachim Ullrich, Xiaoyu Wang, Georg Weidenspointner, Uwe Weierstall, Garth J Williams, Cornelia B Wunderer, Petra Fromme, John C H Spence, Thilo Stehle, Henry N Chapman, Christian Betzel, Michael Duszenko.
Abstract
Protein crystallization in cells has been observed several times in nature. However, owing to their small size these crystals have not yet been used for X-ray crystallographic analysis. We prepared nano-sized in vivo-grown crystals of Trypanosoma brucei enzymes and applied the emerging method of free-electron laser-based serial femtosecond crystallography to record interpretable diffraction data. This combined approach will open new opportunities in structural systems biology.Entities:
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Year: 2012 PMID： 22286384 PMCID： PMC3429599 DOI： 10.1038/nmeth.1859
Source DB: PubMed Journal: Nat Methods ISSN： 1548-7091 Impact factor: 28.547