Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1997-5-8
|
| pubmed:abstractText |
Single crystals of UDP-N-acetylglucosamine enolpyruvyltransferase of Enterobacter cloacae have been grown by vapor diffusion using phosphate buffer as the precipitant. The crystals belong to the monoclinic space group C2 with a = 86.9 A, b = 155.9 A, c = 83.8 A, beta = 91.6 degrees. Assuming two monomers per asymmetric unit, the solvent content of these crystals is 63%. Flash-frozen crystals diffract to beyond 2 A resolution.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
1047-8477
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
117
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
73-6
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:8776890-Alkyl and Aryl Transferases,
pubmed-meshheading:8776890-Crystallization,
pubmed-meshheading:8776890-Crystallography, X-Ray,
pubmed-meshheading:8776890-Enterobacter cloacae,
pubmed-meshheading:8776890-Protein Conformation,
pubmed-meshheading:8776890-Recombinant Proteins,
pubmed-meshheading:8776890-Transferases
|
| pubmed:articleTitle |
Crystallization and preliminary X-ray diffraction analysis of UDP-N-acetylglucosamine enolpyruvyltransferase of Enterobacter cloacae.
|
| pubmed:affiliation |
Max-Planck-Unit for Structural Molecular Biology, Hamburg, Germany.
|
| pubmed:publicationType |
Journal Article
|