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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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Formato: | Texto |
Lenguaje: | English |
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International Union of Crystallography
2007
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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. |
format | Text |
id | pubmed-2330129 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2007 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
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
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title_full | Crystallization and preliminary X-ray diffraction analysis of ω-amino acid:pyruvate transaminase from Chromobacterium violaceum
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title_fullStr | Crystallization and preliminary X-ray diffraction analysis of ω-amino acid:pyruvate transaminase from Chromobacterium violaceum
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title_full_unstemmed | Crystallization and preliminary X-ray diffraction analysis of ω-amino acid:pyruvate transaminase from Chromobacterium violaceum
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title_short | Crystallization and preliminary X-ray diffraction analysis of ω-amino acid:pyruvate transaminase from Chromobacterium violaceum
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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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