Lattice mobility and anomalous temperature factor behaviour in cytochrome c′

B. C. Finzel, F. R. Salemme

Research output: Contribution to journalArticle

20 Scopus citations

Abstract

Atomic temperature factors (B-values) obtained from X-ray refinement experiments provide empirical estimates of protein mobility that have been correlated with both theoretical simulations of protein dynamics1 and experimental studies of antibody reactivity2,3. The comparison of B-values with protein solution properties requires adjustment of the apparent atomic mobilities to compensate for the effects of the crystal environment 4-6. Here we compare crystallographically independent subunits of the dimeric cytochrome c′ from the bacterium Rhodospirillum molischianum to examine how lattice effects influence refined B-values. In addition to local effects on protein mobility at crystal contacts4,5, we show that B-value differences up to 12 å2 between subunits result from lattice disordering effects that approximate to concerted rotations of the molecules about a crystal symmetry axis.

Original languageEnglish (US)
Pages (from-to)686-688
Number of pages3
JournalNature
Volume315
Issue number6021
DOIs
StatePublished - Dec 1 1985
Externally publishedYes

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