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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1998-9-25
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pubmed:abstractText |
Crystallographic studies of ribosomal proteins from bacteria progressed rapidly during the last decade, though the structures of ribosomal proteins from other kingdoms have not yet been published. Here we describe crystals of archaeal ribosomal protein L1 from Methanococcus jannaschii. The protein crystals were grown in 10% PEG 10 K, 50 mM Hepes-HCl (pH 7.5) in hanging drops equilibrated against 33% PEG 10 K, 100 mM Hepes-HCl (pH 7.5). The crystals diffract to at least 2.5 A resolution and belong to the space group P1 with cell parameters a = 34.09 A, b = 39.39 A, c = 55.84 A, alpha = 83.65 degrees, beta = 80.38 degrees, gamma = 75.37 degrees.
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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
|
pubmed:month |
Jun
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pubmed:issn |
1039-9712
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
45
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
349-54
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading | |
pubmed:year |
1998
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pubmed:articleTitle |
Crystals of ribosomal protein L1 from a hyperthermophilic archaeon Methanococcus jannaschii.
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pubmed:affiliation |
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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