spacer
spacer

PDBsum entry 5o4c

Go to PDB code: 
Top Page protein ligands metals Protein-protein interface(s) links
Membrane protein PDB id
5o4c
Contents
Protein chains
332 a.a.
258 a.a.
273 a.a.
323 a.a.
Ligands
HEC ×4
DGA
SO4 ×12
LDA ×4
HTO ×2
BCB ×4
BPB ×2
MQ7
NS5
Metals
FE2
Waters ×13

References listed in PDB file
Key reference
Title From macrocrystals to microcrystals: a strategy for membrane protein serial crystallography.
Authors R.Dods, P.Båth, D.Arnlund, K.R.Beyerlein, G.Nelson, M.Liang, R.Harimoorthy, P.Berntsen, E.Malmerberg, L.Johansson, R.Andersson, R.Bosman, S.Carbajo, E.Claesson, C.E.Conrad, P.Dahl, G.Hammarin, M.S.Hunter, C.Li, S.Lisova, D.Milathianaki, J.Robinson, C.Safari, A.Sharma, G.Williams, C.Wickstrand, O.Yefanov, J.Davidsson, D.P.Deponte, A.Barty, G.Brändén, R.Neutze.
Ref. Structure, 2017, 25, 1461. [DOI no: 10.1016/j.str.2017.07.002]
PubMed id 28781082
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 RCvirserial 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.
PROCHECK
Go to PROCHECK summary
 Headers

 

spacer

spacer