Data on the optimizations of expression and purification of human BiP/GRP78 protein in Escherichia coli

Human BiP/GRP78 is involved in the folding and assembly of proteins in the endoplasmic reticulum. The proteins for crystallization in good amount and quality are prerequisites for obtaining ideal crystals. To meet these requirements, different BiP/GRP78 constructs, competent cells, vectors, and conc...

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Detalles Bibliográficos
Autores principales: Yang, Jiao, Zhou, Lei, Liu, Qinglian
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2016
Materias:
Data Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5219641/
https://www.ncbi.nlm.nih.gov/pubmed/28070540
http://dx.doi.org/10.1016/j.dib.2016.08.006
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author Yang, Jiao
Zhou, Lei
Liu, Qinglian
author_facet Yang, Jiao
Zhou, Lei
Liu, Qinglian
author_sort Yang, Jiao
collection PubMed
description Human BiP/GRP78 is involved in the folding and assembly of proteins in the endoplasmic reticulum. The proteins for crystallization in good amount and quality are prerequisites for obtaining ideal crystals. To meet these requirements, different BiP/GRP78 constructs, competent cells, vectors, and concentrations of inducer were tested in order to obtain soluble BiP/GRP78 protein with the highest amount and best purity. The BiP–T229A–L(3,4′)–Smt3 fusion protein was expressed in a soluble manner and finally purified with the highest purity using size exclusion chromatography, which was suitable for further protein crystallization.
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spelling pubmed-52196412017-01-09 Data on the optimizations of expression and purification of human BiP/GRP78 protein in Escherichia coli Yang, Jiao Zhou, Lei Liu, Qinglian Data Brief Data Article Human BiP/GRP78 is involved in the folding and assembly of proteins in the endoplasmic reticulum. The proteins for crystallization in good amount and quality are prerequisites for obtaining ideal crystals. To meet these requirements, different BiP/GRP78 constructs, competent cells, vectors, and concentrations of inducer were tested in order to obtain soluble BiP/GRP78 protein with the highest amount and best purity. The BiP–T229A–L(3,4′)–Smt3 fusion protein was expressed in a soluble manner and finally purified with the highest purity using size exclusion chromatography, which was suitable for further protein crystallization. Elsevier 2016-08-09 /pmc/articles/PMC5219641/ /pubmed/28070540 http://dx.doi.org/10.1016/j.dib.2016.08.006 Text en © 2016 Published by Elsevier Inc. http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Data Article
Yang, Jiao
Zhou, Lei
Liu, Qinglian
Data on the optimizations of expression and purification of human BiP/GRP78 protein in Escherichia coli
title Data on the optimizations of expression and purification of human BiP/GRP78 protein in Escherichia coli
title_full Data on the optimizations of expression and purification of human BiP/GRP78 protein in Escherichia coli
title_fullStr Data on the optimizations of expression and purification of human BiP/GRP78 protein in Escherichia coli
title_full_unstemmed Data on the optimizations of expression and purification of human BiP/GRP78 protein in Escherichia coli
title_short Data on the optimizations of expression and purification of human BiP/GRP78 protein in Escherichia coli
title_sort data on the optimizations of expression and purification of human bip/grp78 protein in escherichia coli
topic Data Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5219641/
https://www.ncbi.nlm.nih.gov/pubmed/28070540
http://dx.doi.org/10.1016/j.dib.2016.08.006
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