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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 5
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pubmed:dateCreated |
2006-3-2
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pubmed:abstractText |
The human gene coding for the enhancer of rudimentary homologue (ERH) protein was overexpressed in Escherichia coli. The ERH protein was purified by anion-exchange, hydrophobic interaction and gel-filtration chromatography. Well diffracting single crystals were obtained by the vapour-diffusion method in hanging drops. The crystals belong to the trigonal space group P3(1)21 or its enantiomorph P3(2)21, with unit-cell parameters a = b = 53.74, c = 67.45 A, alpha = beta = 90, gamma = 120 degrees. They diffract to at least 1.75 A. A selenomethionine derivative of the protein was prepared and crystallized for multiwavelength anomalous diffraction (MAD) phasing.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1744-3091
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
61
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
531-3
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
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pubmed:year |
2005
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pubmed:articleTitle |
Overproduction, purification, crystallization and preliminary X-ray diffraction studies of the human transcription repressor ERH.
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pubmed:affiliation |
Department of Biology, Illinois Institute of Technology, Chicago, IL 60616, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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