Source:http://linkedlifedata.com/resource/pubmed/id/10666581
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 12
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pubmed:dateCreated |
2000-3-17
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pubmed:abstractText |
Crystals of the Escherichia coli UDP-MurNAc-tripeptide D-Ala-D-Ala-adding protein (MurF), which catalyzes the formation of the last metabolite of the bacterial cell-wall building block, have been grown in hanging-drop vapor-diffusion trials using PEG 8K as a precipitating agent. The crystals belong to hexagonal space group P6(1) or P6(5), with unit-cell dimensions a = b = 74, c = 425 A. The asymmetric unit contains two molecules, with a crystal volume per protein mass (V(m)) of 3.4 A(3) Da(-1) and a solvent content of about 64% by volume. A native data set to 2.8 A resolution has been obtained from a frozen crystal using a synchrotron X-ray source.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0907-4449
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
55
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2033-4
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pubmed:dateRevised |
2007-7-24
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pubmed:meshHeading |
pubmed-meshheading:10666581-Base Sequence,
pubmed-meshheading:10666581-Crystallization,
pubmed-meshheading:10666581-Crystallography, X-Ray,
pubmed-meshheading:10666581-DNA Primers,
pubmed-meshheading:10666581-Escherichia coli,
pubmed-meshheading:10666581-Gene Expression,
pubmed-meshheading:10666581-Peptide Synthases,
pubmed-meshheading:10666581-Recombinant Proteins
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pubmed:year |
1999
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pubmed:articleTitle |
Crystallization and preliminary X-ray analysis of the Escherichia coli UDP-MurNAc-tripeptide D-alanyl-D-alanine-adding enzyme (MurF).
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pubmed:affiliation |
Department of Antiviral Research, Merck Research Laboratories, West Point, PA 19486, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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