title: Crystallization and preliminary X-ray diffraction studies of human catalase.
abstract: The enzyme catalase (H(2)O(2)-H(2)O(2) oxidoredutase; E.C. 11.1.6) was purified from haemolysate of human placenta and crystallized using the vapour-diffusion 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 A. A molecular-replacement solution of the structure has been obtained using beef liver catalase (PDB code 4blc) as a search model.
authors.affiliation: Laboratório Nacional de Luz Síncrotron, Caixa Postal 6192, CEP 13083-970, Campinas SP, Brazil and Depto. Física, UNICAMP, Caixa Postal 6165, CEP, 13083-970, Campinas SP, Brazil.
authors.forename: R A
authors.initials: RA
authors.lastname: Nagem
authors.forename: E A
authors.initials: EA
authors.lastname: Martins
authors.forename: V M
authors.initials: VM
authors.lastname: Gonçalves
authors.forename: R
authors.initials: R
authors.lastname: Aparício
authors.forename: I
authors.initials: I
authors.lastname: Polikarpov
mesh_terms: D002374:Catalase / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D006801:Humans; D010920:Placenta / Q000201:enzymology; D011257:Pregnancy Proteins / Q000737:chemistry; D014961:X-Ray Diffraction
chemical_list: D011257:Pregnancy Proteins; D002374:Catalase