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Title: Purification, crystallization and preliminary X-ray crystallographic studies of Rv3705c from Mycobacterium tuberculosis

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.
Authors:
 [1] ;  [2] ;  [1] ;  [2] ;  [3] ;  [1]
  1. East China University of Science and Technology, 130 Meilong Road, Shanghai 200237, People’s Republic of (China)
  2. Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, People’s Republic of (China)
  3. Center for Tuberculosis Control of Guangdong Province, Guangzhou, People’s Republic of (China)
Publication Date:
OSTI Identifier:
22375696
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta crystallographica. Section F, Structural biology communications; Journal Volume: 70; Journal 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)
Country of Publication:
United States
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; CRYSTALS; DIFFUSION; PROTEINS; RESOLUTION; SPACE GROUPS; X-RAY DIFFRACTION