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Crystallization and preliminary X-ray diffraction analysis of ω-amino acid:pyruvate transaminase from Chromobacterium violaceum

The enzyme ω-transaminase catalyses the conversion of chiral ω-amines to ketones. The recombinant enzyme from Chromobacterium violaceum has been purified to homogeneity. The enzyme was crystallized from PEG 4000 using the microbatch method. Data were collected to 1.7 Å resolution from a crystal belo...

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Detalles Bibliográficos
Autores principales: Sayer, Christopher, Isupov, Michail N., Littlechild, Jennifer A.
Formato: Texto
Lenguaje:English
Publicado: International Union of Crystallography 2007
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2330129/
https://www.ncbi.nlm.nih.gov/pubmed/17277454
http://dx.doi.org/10.1107/S1744309107000863
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author Sayer, Christopher
Isupov, Michail N.
Littlechild, Jennifer A.
author_facet Sayer, Christopher
Isupov, Michail N.
Littlechild, Jennifer A.
author_sort Sayer, Christopher
collection PubMed
description The enzyme ω-transaminase catalyses the conversion of chiral ω-amines to ketones. The recombinant enzyme from Chromobacterium violaceum has been purified to homogeneity. The enzyme was crystallized from PEG 4000 using the microbatch method. Data were collected to 1.7 Å resolution from a crystal belonging to the triclinic space group P1, with unit-cell parameters a = 58.9, b = 61.9, c = 63.9 Å, α = 71.9, β = 87.0, γ = 74.6°. Data were also collected to 1.95 Å from a second triclinic crystal form. The structure has been solved using the molecular-replacement method.
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spelling pubmed-23301292008-05-12 Crystallization and preliminary X-ray diffraction analysis of ω-amino acid:pyruvate transaminase from Chromobacterium violaceum Sayer, Christopher Isupov, Michail N. Littlechild, Jennifer A. Acta Crystallogr Sect F Struct Biol Cryst Commun Crystallization Communications The enzyme ω-transaminase catalyses the conversion of chiral ω-amines to ketones. The recombinant enzyme from Chromobacterium violaceum has been purified to homogeneity. The enzyme was crystallized from PEG 4000 using the microbatch method. Data were collected to 1.7 Å resolution from a crystal belonging to the triclinic space group P1, with unit-cell parameters a = 58.9, b = 61.9, c = 63.9 Å, α = 71.9, β = 87.0, γ = 74.6°. Data were also collected to 1.95 Å from a second triclinic crystal form. The structure has been solved using the molecular-replacement method. International Union of Crystallography 2007-01-17 /pmc/articles/PMC2330129/ /pubmed/17277454 http://dx.doi.org/10.1107/S1744309107000863 Text en © International Union of Crystallography 2007 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
Sayer, Christopher
Isupov, Michail N.
Littlechild, Jennifer A.
Crystallization and preliminary X-ray diffraction analysis of ω-amino acid:pyruvate transaminase from Chromobacterium violaceum
title Crystallization and preliminary X-ray diffraction analysis of ω-amino acid:pyruvate transaminase from Chromobacterium violaceum
title_full Crystallization and preliminary X-ray diffraction analysis of ω-amino acid:pyruvate transaminase from Chromobacterium violaceum
title_fullStr Crystallization and preliminary X-ray diffraction analysis of ω-amino acid:pyruvate transaminase from Chromobacterium violaceum
title_full_unstemmed Crystallization and preliminary X-ray diffraction analysis of ω-amino acid:pyruvate transaminase from Chromobacterium violaceum
title_short Crystallization and preliminary X-ray diffraction analysis of ω-amino acid:pyruvate transaminase from Chromobacterium violaceum
title_sort crystallization and preliminary x-ray diffraction analysis of ω-amino acid:pyruvate transaminase from chromobacterium violaceum
topic Crystallization Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2330129/
https://www.ncbi.nlm.nih.gov/pubmed/17277454
http://dx.doi.org/10.1107/S1744309107000863
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