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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 6
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pubmed:dateCreated |
2000-7-31
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pubmed:abstractText |
This is the first crystallization report of a glycoside hydrolase which belongs to family 82. A recombinant form of His-tagged iota-carrageenase from Alteromonas fortis was expressed, purified and crystallized. Crystals were obtained by the vapour-diffusion method using polyethylene glycol (M(W) = 6000) as a precipitant. They belong to space group P2(1), with unit-cell parameters a = 56. 75, b = 91.04, c = 125.01 A, beta = 93.41 degrees. The unit cell contains two molecules in the asymmetric unit related by a non-crystallographic twofold axis. Crystals diffracted to 2.0 A resolution on a synchrotron beamline.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0907-4449
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
56
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
766-8
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pubmed:dateRevised |
2007-7-24
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pubmed:meshHeading |
pubmed-meshheading:10818359-Alteromonas,
pubmed-meshheading:10818359-Bacterial Proteins,
pubmed-meshheading:10818359-Carrageenan,
pubmed-meshheading:10818359-Crystallization,
pubmed-meshheading:10818359-Crystallography, X-Ray,
pubmed-meshheading:10818359-Gene Expression Regulation, Bacterial,
pubmed-meshheading:10818359-Genes, Bacterial,
pubmed-meshheading:10818359-Glycoside Hydrolases,
pubmed-meshheading:10818359-Recombinant Proteins
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pubmed:year |
2000
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pubmed:articleTitle |
Expression, purification, crystallization and preliminary X-ray analysis of the iota-carrageenase from Alteromonas fortis.
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pubmed:affiliation |
Laboratoire de Cristallographie Macromoléculaire, Institut de Biologie Structurale Jean-Pierre Ebel, CNRS/CEA, Grenoble, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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