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Overexpression, purification and crystallization of a choline-binding protein CbpI from Streptococcus pneumoniae
The choline-binding protein CbpI from Streptococcus pneumoniae is a 23.4 kDa protein with no known function. The protein has been successfully purified initially using Ni–NTA chromatography and to homogeneity using Q-Sepharose ion-exchange resin as an affinity column. CbpI was crystallized using PEG...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
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International Union of Crystallography
2006
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2242943/ https://www.ncbi.nlm.nih.gov/pubmed/16820691 http://dx.doi.org/10.1107/S1744309106020616 |
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author | Paterson, Neil G. Riboldi-Tunicliffe, Alan Mitchell, Timothy J. Isaacs, Neil W. |
author_facet | Paterson, Neil G. Riboldi-Tunicliffe, Alan Mitchell, Timothy J. Isaacs, Neil W. |
author_sort | Paterson, Neil G. |
collection | PubMed |
description | The choline-binding protein CbpI from Streptococcus pneumoniae is a 23.4 kDa protein with no known function. The protein has been successfully purified initially using Ni–NTA chromatography and to homogeneity using Q-Sepharose ion-exchange resin as an affinity column. CbpI was crystallized using PEG 3350 as a precipitant and X-ray crystallographic analysis showed that the crystals belonged to the tetragonal space group P4, with unit-cell parameters a = b = 83.31, c = 80.29 Å, α = β = γ = 90°. The crystal contains two molecules in the asymmetric unit with a solvent content of 55.7% (V (M) = 2.77 Å(3) Da(−1)) and shows a diffraction limit of 3.5 Å. |
format | Text |
id | pubmed-2242943 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2006 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-22429432008-03-13 Overexpression, purification and crystallization of a choline-binding protein CbpI from Streptococcus pneumoniae Paterson, Neil G. Riboldi-Tunicliffe, Alan Mitchell, Timothy J. Isaacs, Neil W. Acta Crystallogr Sect F Struct Biol Cryst Commun Crystallization Communications The choline-binding protein CbpI from Streptococcus pneumoniae is a 23.4 kDa protein with no known function. The protein has been successfully purified initially using Ni–NTA chromatography and to homogeneity using Q-Sepharose ion-exchange resin as an affinity column. CbpI was crystallized using PEG 3350 as a precipitant and X-ray crystallographic analysis showed that the crystals belonged to the tetragonal space group P4, with unit-cell parameters a = b = 83.31, c = 80.29 Å, α = β = γ = 90°. The crystal contains two molecules in the asymmetric unit with a solvent content of 55.7% (V (M) = 2.77 Å(3) Da(−1)) and shows a diffraction limit of 3.5 Å. International Union of Crystallography 2006-06-10 /pmc/articles/PMC2242943/ /pubmed/16820691 http://dx.doi.org/10.1107/S1744309106020616 Text en © International Union of Crystallography 2006 http://journals.iucr.org/services/termsofuse.html This is an open-access article distributed under the terms described at http://journals.iucr.org/services/termsofuse.html. |
spellingShingle | Crystallization Communications Paterson, Neil G. Riboldi-Tunicliffe, Alan Mitchell, Timothy J. Isaacs, Neil W. Overexpression, purification and crystallization of a choline-binding protein CbpI from Streptococcus pneumoniae |
title | Overexpression, purification and crystallization of a choline-binding protein CbpI from Streptococcus pneumoniae
|
title_full | Overexpression, purification and crystallization of a choline-binding protein CbpI from Streptococcus pneumoniae
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title_fullStr | Overexpression, purification and crystallization of a choline-binding protein CbpI from Streptococcus pneumoniae
|
title_full_unstemmed | Overexpression, purification and crystallization of a choline-binding protein CbpI from Streptococcus pneumoniae
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title_short | Overexpression, purification and crystallization of a choline-binding protein CbpI from Streptococcus pneumoniae
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title_sort | overexpression, purification and crystallization of a choline-binding protein cbpi from streptococcus pneumoniae |
topic | Crystallization Communications |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2242943/ https://www.ncbi.nlm.nih.gov/pubmed/16820691 http://dx.doi.org/10.1107/S1744309106020616 |
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