Publication

Article Metrics

Citations


Online attention

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 DOI Help
PMID: 25195908 PMID Help

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 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 = 220.74 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