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PDBsum entry 5o4c

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protein ligands metals Protein-protein interface(s) links
Membrane protein PDB id
5o4c

 

 

 

 

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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
PDB id:
5o4c
Name: Membrane protein
Title: From macrocrystals to microcrystals: a strategy for membrane protein serial crystallography
Structure: Photosynthetic reaction center cytochromE C subunit. Chain: c. Synonym: cytochrome c558/c559. Reaction center protein h chain. Chain: h. Synonym: photosynthetic reaction center h subunit. Reaction center protein l chain. Chain: l. Synonym: photosynthetic reaction center l subunit.
Source: Blastochloris viridis. Organism_taxid: 1079. Organism_taxid: 1079
Resolution:
2.80Å     R-factor:   0.167     R-free:   0.196
Authors: R.Dods,P.Baath,G.Branden,R.Neutze
Key ref: R.Dods et al. (2017). From Macrocrystals to Microcrystals: A Strategy for Membrane Protein Serial Crystallography. Structure, 25, 1461. PubMed id: 28781082 DOI: 10.1016/j.str.2017.07.002
Date:
28-May-17     Release date:   16-Aug-17    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P07173  (CYCR_BLAVI) -  Photosynthetic reaction center cytochrome c subunit from Blastochloris viridis
Seq:
Struc:
356 a.a.
332 a.a.
Protein chain
Pfam   ArchSchema ?
P06008  (RCEH_BLAVI) -  Reaction center protein H chain from Blastochloris viridis
Seq:
Struc:
258 a.a.
258 a.a.*
Protein chain
Pfam   ArchSchema ?
P06009  (RCEL_BLAVI) -  Reaction center protein L chain from Blastochloris viridis
Seq:
Struc:
274 a.a.
273 a.a.
Protein chain
Pfam   ArchSchema ?
P06010  (RCEM_BLAVI) -  Reaction center protein M chain from Blastochloris viridis
Seq:
Struc:
324 a.a.
323 a.a.
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 1 residue position (black cross)

 

 
DOI no: 10.1016/j.str.2017.07.002 Structure 25:1461 (2017)
PubMed id: 28781082  
 
 
From Macrocrystals to Microcrystals: A Strategy for Membrane Protein Serial Crystallography.
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.
 
  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.
 

 

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