Is the bond-valence method able to identify metal atoms in protein structures?

The proper assignment of metal ions in X‐ray structures of proteins is not always easy, but in many cases this knowledge can be important, e.g. for an understanding of enzyme mechanism. In this publication, the bond‐valence approach is assessed critically. A simplified version, the calcium bond‐vale...

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Bibliographic Details
Published inActa crystallographica. Section D, Biological crystallography. Vol. 59; no. 1; pp. 32 - 37
Main Authors Müller, Peter, Köpke, Sinje, Sheldrick, George M.
Format Journal Article
LanguageEnglish
Published 5 Abbey Square, Chester, Cheshire CH1 2HU, England Munksgaard International Publishers 01.01.2003
Subjects
Algorithms
Binding Sites
bond-valence method
Calcium - chemistry
Calcium - metabolism
CBVS
metal ions in proteins
Metalloproteins - chemistry
Metalloproteins - metabolism
Metals - chemistry
Metals - metabolism
Models, Chemical
Sensitivity and Specificity
SHELXPRO
Statistical Distributions
validation
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Summary:The proper assignment of metal ions in X‐ray structures of proteins is not always easy, but in many cases this knowledge can be important, e.g. for an understanding of enzyme mechanism. In this publication, the bond‐valence approach is assessed critically. A simplified version, the calcium bond‐valence sum (CBVS), is proposed for the convenient analysis of the geometric environment of potential sites with a view to metal‐ion assignment. The bond‐valence approach is found to be more reliable for structures determined from high‐resolution data (1.5 Å or better).
Bibliography:ark:/67375/WNG-FKQ927LK-Z
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ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444902018000