%0 Journal Article %J Acta Crystallogr D Biol Crystallogr %D 2003 %T Crystallization and preliminary X-ray diffraction analysis of the di-haem cytochrome c peroxidase from Pseudomonas stutzeri %A Bonifacio, C. %A Cunha, CA %A Muller, A. %A Timoteo, C. G. %A Dias, JM %A Moura, I %A Romao, MJ %K Crystallization/methods %K Crystallography, X-Ray %K Cytochrome-c Peroxidase/*chemistry %K Dimerization %K Heme/*chemistry %K Models, Molecular %K Pseudomonas/*enzymology %K Synchrotrons %M 12554948 %P 345-7 %U http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12554948 %V 59 %X

Crystals of cytochrome c peroxidase from Pseudomonas stutzeri were obtained using sodium citrate and PEG 8000 as precipitants. A complete data set was collected to a resolution of 1.6 A under cryogenic conditions using synchrotron radiation at the ESRF. The crystals belong to space group P2(1), with unit-cell parameters a = 69.29, b = 143.31, c = 76.83 A, beta = 100.78 degrees. Four CCP molecules were found in the asymmetric unit, corresponding to a pair of dimers related by local dyads. The crystal packing in the structure shows that the functional dimers can dimerize, as suggested by previous biochemical studies.

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Journal ArticleResearch Support, Non-U.S. Gov'tDenmark

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