Crystallization and preliminary X-ray diffraction analysis of a soluble domain of the putative zinc transporter CzrB from Thermus thermophilus
- Department of Chemical and Environmental Sciences and Materials and Surface Science Institute, University of Limerick, Limerick (Ireland)
- Department of Chemistry, The Ohio State University, Columbus, OH 43210 (United States)
- Cornell High Energy Synchrotron Source, Cornell University, Ithaca, NY 14850 (United States)
Diffraction-quality crystals of the apo (1.7 Å) and zinc-bound forms (2.2 Å) of the water-soluble C-terminal domain of the putative zinc transporter CzrB from T. thermophilus have been grown using recombinant production of the protein in E. coli and a combination of vapour-diffusion, batch and seeding crystallogenesis techniques. CzrB is a putative zinc transporter from Thermus thermophilus. The protein is proposed to consist of a hexahelical transmembrane domain with a cytosolic extramembranal C-terminus. The latter 92-residue fragment may be expressed free and may function independently of the full-length integral membrane protein. A 6×His-tagged form of the water-soluble fragment has been overexpressed in Escherichia coli and diffraction-quality crystals of the tagged and tag-free variants have been grown. Preliminary X-ray analyses of tag-free fragment crystals with (2.2 Å resolution) and without zinc ions (1.7 Å resolution) reveal that the former has at least two zinc ions bound per monomer.
- OSTI ID:
- 22360389
- Journal Information:
- Acta Crystallographica. Section F, Vol. 63, Issue Pt 8; Other Information: PMCID: PMC2335163; PMID: 17671365; PUBLISHER-ID: gj5025; OAI: oai:pubmedcentral.nih.gov:2335163; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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