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

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 P6(1)22 or P6(5)22, with unit-cell parameters a = b = 198.0, c =...

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Autores principales: Lu, Feifei, Gao, Feng, Li, Honglin, Gong, Weimin, Zhou, Lin, Bi, Lijun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2014
Materias:
Crystallization Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4118811/
https://www.ncbi.nlm.nih.gov/pubmed/25084389
http://dx.doi.org/10.1107/S2053230X14014113
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author Lu, Feifei
Gao, Feng
Li, Honglin
Gong, Weimin
Zhou, Lin
Bi, Lijun
author_facet Lu, Feifei
Gao, Feng
Li, Honglin
Gong, Weimin
Zhou, Lin
Bi, Lijun
author_sort Lu, Feifei
collection PubMed
description 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 P6(1)22 or P6(5)22, 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.
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spelling pubmed-41188112014-08-15 Purification, crystallization and preliminary X-ray crystallographic studies of Rv3705c from Mycobacterium tuberculosis Lu, Feifei Gao, Feng Li, Honglin Gong, Weimin Zhou, Lin Bi, Lijun Acta Crystallogr F Struct Biol Commun Crystallization Communications 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 P6(1)22 or P6(5)22, 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. International Union of Crystallography 2014-07-23 /pmc/articles/PMC4118811/ /pubmed/25084389 http://dx.doi.org/10.1107/S2053230X14014113 Text en © Lu et al. 2014 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
spellingShingle Crystallization Communications
Lu, Feifei
Gao, Feng
Li, Honglin
Gong, Weimin
Zhou, Lin
Bi, Lijun
Purification, crystallization and preliminary X-ray crystallographic studies of Rv3705c from Mycobacterium tuberculosis
title Purification, crystallization and preliminary X-ray crystallographic studies of Rv3705c from Mycobacterium tuberculosis
title_full Purification, crystallization and preliminary X-ray crystallographic studies of Rv3705c from Mycobacterium tuberculosis
title_fullStr Purification, crystallization and preliminary X-ray crystallographic studies of Rv3705c from Mycobacterium tuberculosis
title_full_unstemmed Purification, crystallization and preliminary X-ray crystallographic studies of Rv3705c from Mycobacterium tuberculosis
title_short Purification, crystallization and preliminary X-ray crystallographic studies of Rv3705c from Mycobacterium tuberculosis
title_sort purification, crystallization and preliminary x-ray crystallographic studies of rv3705c from mycobacterium tuberculosis
topic Crystallization Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4118811/
https://www.ncbi.nlm.nih.gov/pubmed/25084389
http://dx.doi.org/10.1107/S2053230X14014113
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