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

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

UN SDGs

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 = "John Wiley and Sons Ltd",

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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 - 1744-3091

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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