期刊
STRUCTURE
卷 25, 期 9, 页码 1461-+出版社
CELL PRESS
DOI: 10.1016/j.str.2017.07.002
关键词
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资金
- U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-AC02-76SF00515]
- NIH [P41GM103393]
- European Commission Marie Curie Training Network NanoMem
- Swedish Research Council [2015-00560, 349-2011-6485]
- Swedish Foundation for Strategic Research [SRL10-0036]
- Knut and Alice Wallenberg Foundation [KAW 2012.0284, KAW 2014.0275, KAW 2012.0106]
- Swedish Research Council [2015-00560] Funding Source: Swedish Research Council
- Swedish Foundation for Strategic Research (SSF) [SRL10-0036] Funding Source: Swedish Foundation for Strategic Research (SSF)
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-angstrom to 2.4-angstrom resolution. This approach may allow known crystallization conditions for other proteins to be adapted to exploit novel scientific opportunities created by serial crystallography.
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