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^*

^*Corresponding author for this work

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

2 Scopus citations

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. 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.

Original language	English
Pages (from-to)	107-109
Number of pages	3
Journal	Acta Crystallographica Section F:Structural Biology Communications
Volume	71
DOIs	https://doi.org/10.1107/S2053230X14027228
State	Published - 1 Jan 2015
Externally published	Yes

Keywords

Mycobacterium tuberculosis
Rv3899c

UN SDGs

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

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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",

volume = "71",

pages = "107--109",

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

issn = "1744-3091",

publisher = "John Wiley and Sons Ltd",

}

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 Communications

JF - Acta Crystallographica Section F:Structural Biology Communications

ER -

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

Abstract

Keywords

UN SDGs

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