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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
|
| pubmed:dateCreated |
1994-3-15
|
| pubmed:abstractText |
The catalytic domain of a thermostable xylanase from Clostridium thermocellum has been expressed in Escherichia coli and crystallized from a polyethylene glycol 2000 solution by the hanging drop method. Crystals belong to the triclinic space group P1 with cell dimensions a = 46.8 A, b = 50.8 A, c = 70.3 A, alpha = 100.7 degrees, beta = 83.8 degrees, gamma = 101.6 degrees, and two molecules in the unit cell. These crystals diffract X-rays to at least 1.8 A resolution and are suitable for high-resolution X-ray analysis.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jan
|
| pubmed:issn |
0022-2836
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
28
|
| pubmed:volume |
235
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1348-50
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:8308898-Amino Acid Sequence,
pubmed-meshheading:8308898-Binding Sites,
pubmed-meshheading:8308898-Catalysis,
pubmed-meshheading:8308898-Clostridium,
pubmed-meshheading:8308898-Crystallization,
pubmed-meshheading:8308898-Crystallography, X-Ray,
pubmed-meshheading:8308898-Endo-1,4-beta Xylanases,
pubmed-meshheading:8308898-Glycoside Hydrolases,
pubmed-meshheading:8308898-Molecular Sequence Data
|
| pubmed:year |
1994
|
| pubmed:articleTitle |
Crystallization and preliminary diffraction analysis of the catalytic domain of xylanase Z from Clostridium thermocellum.
|
| pubmed:affiliation |
Unité d'Immunologie Structurale, URA 359 CNRS, Institut Pasteur, Paris, France.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|