Crystallization and preliminary X-ray diffraction analysis of the amidase domain of allophanate hydrolase from Pseudomonas sp. strain ADP

The allophanate hydrolase from Pseudomonas sp. strain ADP was expressed and purified, and a tryptic digest fragment was subsequently identified, expressed and purified. This 50 kDa construct retained amidase activity and was crystallized. The crystals diffracted to 2.5 Å resolution and adopted space...

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Autores principales: Balotra, Sahil, Newman, Janet, French, Nigel G., Briggs, Lyndall J., Peat, Thomas S., Scott, Colin
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/PMC3944691/
https://www.ncbi.nlm.nih.gov/pubmed/24598916
http://dx.doi.org/10.1107/S2053230X13034705
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author Balotra, Sahil
Newman, Janet
French, Nigel G.
Briggs, Lyndall J.
Peat, Thomas S.
Scott, Colin
author_facet Balotra, Sahil
Newman, Janet
French, Nigel G.
Briggs, Lyndall J.
Peat, Thomas S.
Scott, Colin
author_sort Balotra, Sahil
collection PubMed
description The allophanate hydrolase from Pseudomonas sp. strain ADP was expressed and purified, and a tryptic digest fragment was subsequently identified, expressed and purified. This 50 kDa construct retained amidase activity and was crystallized. The crystals diffracted to 2.5 Å resolution and adopted space group P2(1), with unit-cell parameters a = 82.4, b = 179.2, c = 112.6 Å, β = 106.6°.
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spelling pubmed-39446912014-03-12 Crystallization and preliminary X-ray diffraction analysis of the amidase domain of allophanate hydrolase from Pseudomonas sp. strain ADP Balotra, Sahil Newman, Janet French, Nigel G. Briggs, Lyndall J. Peat, Thomas S. Scott, Colin Acta Crystallogr F Struct Biol Commun Crystallization Communications The allophanate hydrolase from Pseudomonas sp. strain ADP was expressed and purified, and a tryptic digest fragment was subsequently identified, expressed and purified. This 50 kDa construct retained amidase activity and was crystallized. The crystals diffracted to 2.5 Å resolution and adopted space group P2(1), with unit-cell parameters a = 82.4, b = 179.2, c = 112.6 Å, β = 106.6°. International Union of Crystallography 2014-02-19 /pmc/articles/PMC3944691/ /pubmed/24598916 http://dx.doi.org/10.1107/S2053230X13034705 Text en © Balotra 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
Balotra, Sahil
Newman, Janet
French, Nigel G.
Briggs, Lyndall J.
Peat, Thomas S.
Scott, Colin
Crystallization and preliminary X-ray diffraction analysis of the amidase domain of allophanate hydrolase from Pseudomonas sp. strain ADP
title Crystallization and preliminary X-ray diffraction analysis of the amidase domain of allophanate hydrolase from Pseudomonas sp. strain ADP
title_full Crystallization and preliminary X-ray diffraction analysis of the amidase domain of allophanate hydrolase from Pseudomonas sp. strain ADP
title_fullStr Crystallization and preliminary X-ray diffraction analysis of the amidase domain of allophanate hydrolase from Pseudomonas sp. strain ADP
title_full_unstemmed Crystallization and preliminary X-ray diffraction analysis of the amidase domain of allophanate hydrolase from Pseudomonas sp. strain ADP
title_short Crystallization and preliminary X-ray diffraction analysis of the amidase domain of allophanate hydrolase from Pseudomonas sp. strain ADP
title_sort crystallization and preliminary x-ray diffraction analysis of the amidase domain of allophanate hydrolase from pseudomonas sp. strain adp
topic Crystallization Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3944691/
https://www.ncbi.nlm.nih.gov/pubmed/24598916
http://dx.doi.org/10.1107/S2053230X13034705
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