Recombinant expression, purification, crystallization and preliminary X-ray diffraction analysis of the C-terminal DUF490(963-1138) domain of TamB from Escherichia coli.
Acta Crystallogr F Struct Biol Commun
; 70(Pt 9): 1272-5, 2014 Sep.
Article
en En
| MEDLINE
| ID: mdl-25195908
ABSTRACT
TamB is a recently described inner membrane protein that, together with its partner protein TamA, is required for the efficient secretion of a subset of autotransporter proteins in Gram-negative bacteria. In this study, the C-terminal DUF490963-1138 domain of TamB was overexpressed in Escherichia coli K-12, purified and crystallized using the sitting-drop vapour-diffusion method. The crystals belonged to the primitive trigonal space group P3121, with unit-cell parameters a = b = 57.34, c = 220.74â
Å, and diffracted to 2.1â
Å resolution. Preliminary secondary-structure and X-ray diffraction analyses are reported. Two molecules are predicted to be present in the asymmetric unit. Experimental phasing using selenomethionine-labelled protein will be undertaken in the future.
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1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Cristalografía por Rayos X
/
Proteínas de Escherichia coli
Idioma:
En
Revista:
Acta Crystallogr F Struct Biol Commun
Año:
2014
Tipo del documento:
Article
País de afiliación:
Reino Unido