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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 11
pubmed:dateCreated
2009-11-20
pubmed:abstractText
The intracellular beta-glucosidase from Kluyveromyces marxianus NBRC1777 (KmBglI) belongs to glycoside hydrolase family 3 and has a unique domain architecture. Selenomethionine-labelled KmBglI was purified and crystallized by the hanging-drop vapour-diffusion method using the purified enzyme at 30 mg ml(-1), 0.04 M potassium dihydrogen phosphate pH 5.1, 16%(w/v) PEG 8000 and 20%(v/v) glycerol. The crystal belonged to space group C2, with unitcell parameters a = 245.8, b = 148.7, c = 119.9 angstrom, beta = 112.9 degrees. Multiple-wavelength anomalous dispersion data were collected at 2.4 and 2.5 angstrom resolution. A tetramer was assumed to be present in the asymmetric unit, which gave a Matthews coefficient of 2.6 angstrom(3) Da(-1).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1744-3091
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
65
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1190-2
pubmed:dateRevised
2011-11-1
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Purification, crystallization and preliminary X-ray analysis of beta-glucosidase from Kluyveromyces marxianus NBRC1777.
pubmed:affiliation
Research Institute for Bioresources and Biotechnology, Ishikawa Prefectural University, Nonoichi, Ishikawa, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't