Purification, crystallization and preliminary X-ray crystallographic studies of Rv3705c from Mycobacterium tuberculosis
Journal Article
·
· Acta crystallographica. Section F, Structural biology communications
- East China University of Science and Technology, 130 Meilong Road, Shanghai 200237, People’s Republic of (China)
- Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, People’s Republic of (China)
- Center for Tuberculosis Control of Guangdong Province, Guangzhou, People’s Republic of (China)
The cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of Rv3705c from M. tuberculosis are described. The conserved protein Rv3705c from Mycobacterium tuberculosis has been cloned, expressed, purified and crystallized by the sitting-drop vapour-diffusion method using PEG 3350 as a precipitant. The Rv3705c crystals exhibited space group P6{sub 1}22 or P6{sub 5}22, with unit-cell parameters a = b = 198.0, c = 364.1 Å, α = β = 90, γ = 120°, and diffracted to a resolution of 3.3 Å.
- OSTI ID:
- 22375696
- Journal Information:
- Acta crystallographica. Section F, Structural biology communications, Vol. 70, Issue Pt 8; Other Information: PMCID: PMC4118811; PMID: 25084389; PUBLISHER-ID: hc5173; OAI: oai:pubmedcentral.nih.gov:4118811; Copyright (c) Lu et al. 2014; This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.; Country of input: International Atomic Energy Agency (IAEA); ISSN 2053-230X
- Country of Publication:
- United States
- Language:
- English
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