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

ABSTRACT: 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 P6122 or P6522, with unit-cell parameters a = b = 198.0, c = 364.1?Å, ? = ? = 90, ? = 120°, and diffracted to a resolution of 3.3?Å.

SUBMITTER: Lu F

PROVIDER: S-EPMC4118811 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature

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

Lu Feifei F Gao Feng F Li Honglin H Gong Weimin W Zhou Lin L Bi Lijun L

Acta crystallographica. Section F, Structural biology communications 20140723 Pt 8

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 P6122 or P6522, 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. ...[more]

PMID: 25084389

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