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PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1990-3-20
pubmed:abstractText
The crystal structure of the redox protein pseudoazurin (123 amino acid residues; molecular weight 13,000 daltons) from Alcaligenes faecalis has been refined by fast Fourier restrained least-squares minimization. Cycles of rebuilding were carried out to escape from local minima. Individual isotropic temperature factor values were refined separately for all atoms. The R factor was reduced from 0.400 (for 2647 reflections in the 6.0-2.8 A resolution range) to 0.180 (for all 19,770 reflections in the 9.0-1.55 A resolution range) with a final estimated accuracy in atomic positions of 0.15 A. The final model comprises 917 protein atoms and 93 solvent molecules. The root-mean-square shift of the main-chain atoms between the final and the initial model is 0.94 A (maximum shift 1.8 A). Most of the larger shifts were the result of rebuilding on the graphics system. The average atomic temperature factor, B, is 23.0 A2 for all atoms. Side-chain atoms with high B values were omitted, and their positions checked from difference maps. The three carboxy-terminal residues were omitted from the final model as no single conformation could be assigned from the observed electron density. All other protein atoms were included.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0108-7681
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
44 ( Pt 6)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
628-36
pubmed:dateRevised
2007-7-24
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Refinement of the structure of pseudoazurin from Alcaligenes faecalis S-6 at 1.55 A resolution.
pubmed:affiliation
European Molecular Biology Laboratory (EMBL), Hamburg, Federal Republic of Germany.
pubmed:publicationType
Journal Article