 |
PDBsum entry 3d9b
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Transport protein
|
PDB id
|
|
|
|
3d9b
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
| |
|
|
Acta Crystallogr Sect F Struct Biol Cryst Commun
64:880-885
(2008)
|
|
PubMed id:
|
|
|
|
|
| |
|
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.
|
|
|
|
|
|
|
 |
 |
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
');
}
}
 |