Linked Life Data

10964657

Source:http://linkedlifedata.com/resource/pubmed/id/10964657

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2000-10-3
pubmed:abstractText
The accuracy of the structures of biological macromolecules determined by X-ray crystallography is of fundamental importance, both for the understanding of life processes and for medical applications. The resolution of the structure is thus critical, and is largely determined by the quality of single crystals. Here we report the results of applying a magnetic field and a magnetization force during growth of the snake muscle fructose-1,6-bisphosphatase and human estrogenic 17beta-hydroxysteroid dehydrogenase crystals. For both enzyme proteins, the quality of the crystals improved with repeated assay, and their data sets were collected at significantly higher resolutions. These results coincide with a mechanism involving the reduction of convection, due to both the hydrodynamics within a magnet and the partially reduced gravity induced by a magnetization force. The density difference between the crystal and solution becomes less significant, and the sedimentation speed of the crystals is also reduced in the presence of the magnetization force.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-291X
pubmed:author
pubmed:copyrightInfo
Copyright 2000 Academic Press.
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
275
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
274-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Magnet used for protein crystallization: novel attempts to improve the crystal quality.
pubmed:affiliation
Molecular Endocrinology and Oncology Laboratory, Laval University Medical Center, 2705 Boulevard Laurier, Quebec, Quebec, G1V 4G2, Canada. sxlin@crchul.ulaval.ca
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't