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PDBsum entry 3d9b

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protein metals links
Transport protein PDB id
3d9b

 

 

 

 

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Contents
Protein chain
1045 a.a. *
Metals
_NI
* Residue conservation analysis
PDB id:
3d9b
Name: Transport protein
Title: Symmetric structure of e. Coli acrb
Structure: Acriflavine resistance protein b. Chain: a
Source: Escherichia coli. Organism_taxid: 469008. Strain: bl21(de3)
Resolution:
3.42Å     R-factor:   0.291     R-free:   0.355
Authors: D.Veesler,S.Blangy,C.Cambillau,G.Sciara
Key ref: D.Veesler et al. (2008). There is a baby in the bath water: AcrB contamination is a major problem in membrane-protein crystallization. Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 880-885. PubMed id: 18931428
Date:
27-May-08     Release date:   01-Jul-08    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P31224  (ACRB_ECOLI) -  Multidrug efflux pump subunit AcrB from Escherichia coli (strain K12)
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1049 a.a.
1045 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
Acta Crystallogr Sect F Struct Biol Cryst Commun 64:880-885 (2008)
PubMed id: 18931428  
 
 
There is a baby in the bath water: AcrB contamination is a major problem in membrane-protein crystallization.
D.Veesler, S.Blangy, C.Cambillau, G.Sciara.
 
  ABSTRACT  
 
In the course of a crystallographic study of the Methanosarcina mazei CorA transporter, the membrane protein was obtained with at least 95% purity and was submitted to crystallization trials. Small crystals (<100 microm) were grown that diffracted to 3.42 A resolution and belonged to space group R32, with unit-cell parameters a = b = 145.74, c = 514.0 A. After molecular-replacement attempts using available CorA structures as search models failed to yield a solution, it was discovered that the crystals consisted of an Escherichia coli contaminating protein, acriflavine resistance protein B (AcrB), that was present at less than 5% in the protein preparations. AcrB contamination is a major problem when expressing membrane proteins in E. coli since it binds naturally to immobilized metal-ion affinity chromatography (IMAC) resins. Here, the structure is compared with previously deposited AcrB structures and strategies are proposed to avoid this contamination.
 

 

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