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

Feifei Lu; Feng Gao; Honglin Li; Weimin Gong; Lin Zhou; Lijun Bi

doi:10.1107/S2053230X14014113

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

Feifei Lu
, Feng Gao
, Honglin Li
, Weimin Gong
, Lin Zhou^*
, Lijun Bi

^*Corresponding author for this work

Shanghai Key Laboratory of New Drug Design
East China University of Science and Technology
National Laboratory of Biomacromolecules
Center for Tuberculosis Control of Guangdong Province

Research output: Contribution to journal › Article › peer-review

1 Scopus citations

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, α = β = 90, γ = 120°, and diffracted to a resolution of 3.3 Å.

Original language	English
Pages (from-to)	1090-1092
Number of pages	3
Journal	Acta Crystallographica Section F:Structural Biology Communications
Volume	70
Issue number	8
DOIs	https://doi.org/10.1107/S2053230X14014113
State	Published - Aug 2014
Externally published	Yes

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This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

Mycobacterium tuberculosis
Rv3705c

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10.1107/S2053230X14014113

Cite this

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title = "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 {\AA}, α = β = 90, γ = 120°, and diffracted to a resolution of 3.3 {\AA}.",

keywords = "Mycobacterium tuberculosis, Rv3705c",

author = "Feifei Lu and Feng Gao and Honglin Li and Weimin Gong and Lin Zhou and Lijun Bi",

year = "2014",

month = aug,

doi = "10.1107/S2053230X14014113",

language = "英语",

volume = "70",

pages = "1090--1092",

journal = "Acta Crystallographica Section F:Structural Biology Communications",

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publisher = "International Union of Crystallography",

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TY - JOUR

T1 - Purification, crystallization and preliminary X-ray crystallographic studies of Rv3705c from Mycobacterium tuberculosis

AU - Lu, Feifei

AU - Gao, Feng

AU - Li, Honglin

AU - Gong, Weimin

AU - Zhou, Lin

AU - Bi, Lijun

PY - 2014/8

Y1 - 2014/8

N2 - 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.

AB - 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.

KW - Mycobacterium tuberculosis

KW - Rv3705c

UR - https://www.scopus.com/pages/publications/84905489936

U2 - 10.1107/S2053230X14014113

DO - 10.1107/S2053230X14014113

M3 - 文章

C2 - 25084389

AN - SCOPUS:84905489936

SN - 2053-230X

VL - 70

SP - 1090

EP - 1092

JO - Acta Crystallographica Section F:Structural Biology Communications

JF - Acta Crystallographica Section F:Structural Biology Communications

IS - 8

ER -

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

Abstract

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Keywords

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