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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1989-3-13
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pubmed:abstractText |
Human plasminogen kringle 4 has been crystallized in two different crystal forms: monoclinic, a = 32.78(3), b = 49.17(2), c = 46.27(3) A, beta = 100.67 degrees, space group P2(1), four molecules/unit cell, two molecules/asymmetric unit; orthorhombic, a = 32.09(7), b = 49.14(6), c = 49.47(9) A, space group P2(1)2(1)2, four molecules/unit cell. Both crystal forms have a large protein fraction (66% for monoclinic and 62% for orthorhombic) and diffract x-rays to 2.0 A resolution. A self-rotation function has been calculated with monoclinic data indicating a non-crystallographic 2-fold rotation approximately parallel to a* (peak height of 14.3 x sigma). Cross-rotation function calculations are in progress utilizing the coordinates of the conserved structure of kringle 1 of prothrombin and plasminogen kringle 4.
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pubmed:grant | |
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 |
Feb
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
264
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
1922-3
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2914886-Crystallization,
pubmed-meshheading:2914886-Humans,
pubmed-meshheading:2914886-Pancreatic Elastase,
pubmed-meshheading:2914886-Peptide Fragments,
pubmed-meshheading:2914886-Plasminogen,
pubmed-meshheading:2914886-Protein Conformation,
pubmed-meshheading:2914886-X-Ray Diffraction
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pubmed:year |
1989
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pubmed:articleTitle |
Human plasminogen kringle 4. Crystallization and preliminary diffraction data of two different crystal forms.
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pubmed:affiliation |
Department of Chemistry, Michigan State University, East Lansing 48824.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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