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Recombinant expression, purification, crystallization and preliminary X-ray diffraction analysis of the C-terminal DUF490 (963-1138) domain of TamB from Escherichia coli
DOI:
10.1107/S2053230X14017403
PMID:
25195908
Authors:
Inokentijs
Josts
(University of Glasgow)
,
Rhys
Grinter
(University of Glasgow)
,
Sharon
Kelly
(University of Glasgow)
,
Khedidja
Mosbahi
(University of Glasgow)
,
Aleksander
Roszak
(University of Glasgow)
,
Richard J.
Cogdell
(University of Glasgow)
,
Brian O.
Smith
(University of Glasgow)
,
Olwyn
Byron
(University of Glasgow)
,
Daniel
Walker
(University of Glasgow)
Co-authored by industrial partner:
No
Type:
Journal Paper
Journal:
Acta Crystallographica Section F Structural Biology Communications
, VOL 70
, PAGES 1272 - 1275
State:
Published (Approved)
Published:
September 2014
Diamond Proposal Number(s):
5689
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 DUF4909631138 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 = 220.74 A, and diffracted to 2.1 A 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.
Subject Areas:
Biology and Bio-materials
Instruments:
I03-Macromolecular Crystallography