Crystallization and preliminary X-ray diffraction analysis of a dihaem cytochrome c peroxidase from Paracoccus denitrificans
UNSPECIFIED. (2004) Crystallization and preliminary X-ray diffraction analysis of a dihaem cytochrome c peroxidase from Paracoccus denitrificans. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 60 (Part 2). pp. 331-333. ISSN 0907-4449Full text not available from this repository.
Official URL: http://dx.doi.org/10.1107/S0907444903026519
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.
|Item Type:||Journal Article|
|Subjects:||Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
|Journal or Publication Title:||ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY|
|Number of Pages:||3|
|Page Range:||pp. 331-333|
Actions (login required)