Linked Life Data

12454470

Source:http://linkedlifedata.com/resource/pubmed/id/12454470

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2002-11-27
pubmed:abstractText
The structure of Escherichia coli argininosuccinate synthetase (EAS) has been determined using S-SAD, Se-SAD and S/Se-SIRAS data measured with Cu Kalpha radiation. EAS contains 16 methionines and three cysteines in 455 amino acids. At a wavelength of 1.54 A (Cu Kalpha), the native (S-Met) and derivative (Se-Met) proteins yield anomalous signals of approximately 0.86 and 1.6%, respectively. Highly redundant data were measured to 2.0 A from native and derivative EAS crystals. All three structure determinations were carried out in a highly automated manner using SnB and SOLVE/RESOLVE. Despite the minute Bijvoet differences at 1.54 A, the signal was sufficient to determine the heavy-atom substructure and produce high-quality electron-density maps in all three cases. These maps were readily interpretable by the RESOLVE automated building algorithm, which modeled greater than 75% of all three structures. The success of these methods has profound implications for crystallographers experiencing difficulty with heavy-atom incorporation or with limited access to a synchrotron source.
pubmed:grant
pubmed:language
eng
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:author
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2096-101
pubmed:dateRevised
2007-11-14
pubmed:articleTitle
S-SAD, Se-SAD and S/Se-SIRAS using Cu Kalpha radiation: why wait for synchrotron time?
pubmed:affiliation
Structural Biology and Biochemistry, Research Institute, Hospital for Sick Children, 555 University Avenue, Toronto, Ontario, M5G 1X8, Canada.