| Literature DB >> 28781082 |
Robert Dods1, Petra Båth1, David Arnlund1, Kenneth R Beyerlein2, Garrett Nelson3, Mengling Liang4, Rajiv Harimoorthy1, Peter Berntsen5, Erik Malmerberg6, Linda Johansson7, Rebecka Andersson1, Robert Bosman1, Sergio Carbajo4, Elin Claesson1, Chelsie E Conrad3, Peter Dahl1, Greger Hammarin1, Mark S Hunter4, Chufeng Li3, Stella Lisova3, Despina Milathianaki4, Joseph Robinson4, Cecilia Safari1, Amit Sharma1, Garth Williams4, Cecilia Wickstrand1, Oleksandr Yefanov2, Jan Davidsson8, Daniel P DePonte2, Anton Barty2, Gisela Brändén9, Richard Neutze10.
Abstract
Serial protein crystallography was developed at X-ray free-electron lasers (XFELs) and is now also being applied at storage ring facilities. Robust strategies for the growth and optimization of microcrystals are needed to advance the field. Here we illustrate a generic strategy for recovering high-density homogeneous samples of microcrystals starting from conditions known to yield large (macro) crystals of the photosynthetic reaction center of Blastochloris viridis (RCvir). We first crushed these crystals prior to multiple rounds of microseeding. Each cycle of microseeding facilitated improvements in the RCvir serial femtosecond crystallography (SFX) structure from 3.3-Å to 2.4-Å resolution. This approach may allow known crystallization conditions for other proteins to be adapted to exploit novel scientific opportunities created by serial crystallography.Entities:
Keywords: X-ray free-electron laser; microcrystallography; photosynthetic reaction center; serial femtosecond crystallography
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Year: 2017 PMID： 28781082 DOI： 10.1016/j.str.2017.07.002
Source DB: PubMed Journal: Structure ISSN： 0969-2126 Impact factor: 5.006