Linked Life Data

16511037

Source:http://linkedlifedata.com/resource/pubmed/id/16511037

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 4
pubmed:dateCreated
2006-3-2
pubmed:abstractText
Crystals of human triosephosphate isomerase with two crystal morphologies were obtained using the normal vapour-diffusion technique with identical crystallization conditions. One had a disordered plate shape and the crystals were hollow (crystal form 1). As a result, this form was very fragile, diffracted to 2.8 A resolution and had similar crystallographic parameters to those of the structure 1hti in the Protein Data Bank. The other had a fine needle shape (crystal form 2) and was formed more abundantly than crystal form 1, but was unsuitable for structure analysis. Since the normal vapour-diffusion method could not control the crystal morphology, gel-tube methods, both on earth and under microgravity, were applied for crystallization in order to control and improve the crystal quality. Whereas crystal form 1 was only slightly improved using this method, crystal form 2 was greatly improved and diffracted to 2.2 A resolution. Crystal form 2 contained a homodimer in the asymmetric unit, which was biologically essential. Its overall structure was similar to that of 1hti except for the flexible loop, which was located at the active centre Lys13.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511037-11092933, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511037-11264584, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511037-11468418, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511037-12499533, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511037-12777759, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511037-12832803, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511037-14646131, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511037-15299406, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511037-15299407, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511037-15299496, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511037-8061610, http://linkedlifedata.com/resource/pubmed/commentcorrection/16511037-9261072
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1744-3091
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
61
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
346-9
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Structure of a high-resolution crystal form of human triosephosphate isomerase: improvement of crystals using the gel-tube method.
pubmed:affiliation
Exploratory Research Laboratories, Fujisawa Pharmaceutical Co. Ltd, 5-2-3 Tokodai, Tsukuba, Ibaraki 300-2698, Japan. takayoshi_kinoshita@po.fujisawa.co.jp
pubmed:publicationType
Journal Article, Comparative Study