Crystallization and preliminary X-ray diffraction studies of human catalase

Authors
Nagem, RAP Martins, EAL Goncalves, VM Aparicio, R Polikarpov, I
Citation
Rap. Nagem et al., Crystallization and preliminary X-ray diffraction studies of human catalase, ACT CRYST D, 55, 1999, pp. 1614-1615
Citations number
33
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
55
Year of publication
1999
Part
9
Pages
1614 - 1615
Database
ISI
SICI code
0907-4449(199909)55:<1614:CAPXDS>2.0.ZU;2-W
Abstract
The enzyme catalase (H2O2-H2O2 oxidoreductase; E.C. 11.1.6) was purified fr om haemolysate of human placenta and crystallized using the vapour-diffusio n technique. Synchrotron-radiation diffraction data have been collected to 1.76 A resolution. The enzyme crystallized in the space group P2(1)2(1)2(1) , with unit-cell dimensions a = 83.6, b = 139.4, c = 227.5 Angstrom. A mole cular-replacement solution of the structure has been obtained using beef li ver catalase (PDB code 4blc) as a search model.