Source:http://linkedlifedata.com/resource/pubmed/id/15299818
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
Pt 5
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| pubmed:dateCreated |
2004-8-9
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| pubmed:abstractText |
We have obtained two additional crystal forms of the metal-dependent class II fructose-1,6-bisphosphate aldolase from Escherichia coli. Crystals in the shape of elongated plates have unit-cell dimensions a = 73.4, b = 120.0, c = 190.1 A, orthorhombic space group P2(1)2(1)2(1). Monoclinic prisms have unit-cell dimensions a = 67.7, b = 104.3, c = 52.8 A, beta = 105 degrees, space group P2(1). Diffraction to slightly better than 3.0 A, has been observed for both forms using in-house and synchrotron facilities. These crystal forms may aid the structure solution of this enzyme by presenting additional forms for heavy-atom derivatization. These forms have multiple copies of the enzyme in the asymmetric unit and averaging methods might also be useful in the analysis.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:status |
PubMed-not-MEDLINE
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| pubmed:month |
Sep
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| pubmed:issn |
0907-4449
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
1
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| pubmed:volume |
51
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
833-4
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| pubmed:dateRevised |
2009-9-29
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| pubmed:year |
1995
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| pubmed:articleTitle |
Additional crystal forms of the E. coli class II fructose-1,6-bisphosphate aldolase.
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| pubmed:affiliation |
Department of Chemistry, University of Manchester, England.
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| pubmed:publicationType |
Journal Article
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