Purification, crystallization and preliminary X-ray crystallographic studies of Rv3899c from Mycobacterium tuberculosis

Yingjia Song; Jianghui Liu; De Feng Li; Honglin Li; Shihua Wang; Da Cheng Wang; Jie Zhou; Lijun Bi

doi:10.1107/S2053230X14027228

Purification, crystallization and preliminary X-ray crystallographic studies of Rv3899c from Mycobacterium tuberculosis

Yingjia Song
, Jianghui Liu
, De Feng Li
, Honglin Li
, Shihua Wang
, Da Cheng Wang
, Jie Zhou
, Lijun Bi^*

^*此作品的通讯作者

East China University of Science and Technology
Fujian Agriculture and Forestry University
CAS - Institute of Biophysics
Fourth People's Hospital Foshan

科研成果: 期刊稿件 › 文章 › 同行评审

3 引用（Scopus）

摘要

Rv3899c, a hypothetical protein from Mycobacterium tuberculosis that is conserved within the mycobacteria, is predicted to be secreted and has been found in culture filtrates. Here, Rv3899c has been cloned, expressed in Escherichia coli and purified using standard chromatographic techniques. The hanging-drop vapour-diffusion method with PEG 3350 as a precipitant was used to crystallize the protein. N-terminal sequencing results showed that the amino-acid sequence of the crystallized protein began with GATAG, indicating that it is a fragment containing residues 184-410 of Rv3899c. Rv3899c^184-410 crystals exhibited the symmetry of space group P212121, with unit-cell parameters a = 49.88, b = 54.72, c = 75.52Å, α = β = γ = 90°, and diffracted to a resolution of 1.90Å.

源语言	英语
页（从-至）	107-109
页数	3
期刊	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
卷	71
DOI	https://doi.org/10.1107/S2053230X14027228
出版状态	已出版 - 1 1月 2015
已对外发布	是

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可持续发展目标 3 良好健康与福祉

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10.1107/S2053230X14027228

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@article{73993daef1d54e66852d8d8fec28ec73,

title = "Purification, crystallization and preliminary X-ray crystallographic studies of Rv3899c from Mycobacterium tuberculosis",

abstract = "Rv3899c, a hypothetical protein from Mycobacterium tuberculosis that is conserved within the mycobacteria, is predicted to be secreted and has been found in culture filtrates. Here, Rv3899c has been cloned, expressed in Escherichia coli and purified using standard chromatographic techniques. The hanging-drop vapour-diffusion method with PEG 3350 as a precipitant was used to crystallize the protein. N-terminal sequencing results showed that the amino-acid sequence of the crystallized protein began with GATAG, indicating that it is a fragment containing residues 184-410 of Rv3899c. Rv3899c184-410 crystals exhibited the symmetry of space group P212121, with unit-cell parameters a = 49.88, b = 54.72, c = 75.52{\AA}, α = β = γ = 90°, and diffracted to a resolution of 1.90{\AA}.",

keywords = "Mycobacterium tuberculosis, Rv3899c",

author = "Yingjia Song and Jianghui Liu and Li, \{De Feng\} and Honglin Li and Shihua Wang and Wang, \{Da Cheng\} and Jie Zhou and Lijun Bi",

note = "Publisher Copyright: {\textcopyright} 2015 International Union of Crystallography.",

year = "2015",

month = jan,

day = "1",

doi = "10.1107/S2053230X14027228",

language = "英语",

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

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TY - JOUR

T1 - Purification, crystallization and preliminary X-ray crystallographic studies of Rv3899c from Mycobacterium tuberculosis

AU - Song, Yingjia

AU - Liu, Jianghui

AU - Li, De Feng

AU - Li, Honglin

AU - Wang, Shihua

AU - Wang, Da Cheng

AU - Zhou, Jie

AU - Bi, Lijun

PY - 2015/1/1

Y1 - 2015/1/1

N2 - Rv3899c, a hypothetical protein from Mycobacterium tuberculosis that is conserved within the mycobacteria, is predicted to be secreted and has been found in culture filtrates. Here, Rv3899c has been cloned, expressed in Escherichia coli and purified using standard chromatographic techniques. The hanging-drop vapour-diffusion method with PEG 3350 as a precipitant was used to crystallize the protein. N-terminal sequencing results showed that the amino-acid sequence of the crystallized protein began with GATAG, indicating that it is a fragment containing residues 184-410 of Rv3899c. Rv3899c184-410 crystals exhibited the symmetry of space group P212121, with unit-cell parameters a = 49.88, b = 54.72, c = 75.52Å, α = β = γ = 90°, and diffracted to a resolution of 1.90Å.

AB - Rv3899c, a hypothetical protein from Mycobacterium tuberculosis that is conserved within the mycobacteria, is predicted to be secreted and has been found in culture filtrates. Here, Rv3899c has been cloned, expressed in Escherichia coli and purified using standard chromatographic techniques. The hanging-drop vapour-diffusion method with PEG 3350 as a precipitant was used to crystallize the protein. N-terminal sequencing results showed that the amino-acid sequence of the crystallized protein began with GATAG, indicating that it is a fragment containing residues 184-410 of Rv3899c. Rv3899c184-410 crystals exhibited the symmetry of space group P212121, with unit-cell parameters a = 49.88, b = 54.72, c = 75.52Å, α = β = γ = 90°, and diffracted to a resolution of 1.90Å.

KW - Mycobacterium tuberculosis

KW - Rv3899c

UR - https://www.scopus.com/pages/publications/84921709957

U2 - 10.1107/S2053230X14027228

DO - 10.1107/S2053230X14027228

M3 - 文章

C2 - 25615980

AN - SCOPUS:84921709957

SN - 1744-3091

VL - 71

SP - 107

EP - 109

JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

ER -

Purification, crystallization and preliminary X-ray crystallographic studies of Rv3899c from Mycobacterium tuberculosis

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