Crystallization and preliminary X-ray diffraction analysis of a dihaem cytochrome c peroxidase from Paracoccus denitrificans

A Echalier, C F Goodhew, G W Pettigrew, V Fulop

Research output: Contribution to journalArticlepeer-review

Abstract

Cytochrome c peroxidase was isolated from Paracoccus denitrificans and purified to homogeneity in three steps prior to crystallization. Two different diffraction-quality crystal forms were obtained by the hanging-drop vapour-diffusion method using a number of screening conditions. The best (needle-shaped) crystal form is suitable for structural studies and was grown from solutions containing 20% PEG 8000, 0.1 MTris pH 8.5 and 0.2 M MgCl2. Crystals grew to a maximum length of approximately 0.7 mm and belong to the primitive monoclinic space group P2(1), with unit-cell parameters a = 78.3, b = 51.0, c=167.2 Angstrom, beta = 97.9degrees. After a dehydration step and extensive optimization of the cryocooling conditions, a complete data set was collected to 2.2 Angstrom from a native crystal of the fully oxidized form of the enzyme using synchrotron radiation.

Original languageEnglish
Pages (from-to)331-333
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume60
DOIs
Publication statusPublished - Feb 2004

Fingerprint

Dive into the research topics of 'Crystallization and preliminary X-ray diffraction analysis of a dihaem cytochrome c peroxidase from Paracoccus denitrificans'. Together they form a unique fingerprint.

Cite this