Crystallization And Preliminary X-ray Diffraction Studies Of Human Catalase.

dc.creatorNagem, R A
dc.creatorMartins, E A
dc.creatorGonçalves, V M
dc.creatorAparício, R
dc.creatorPolikarpov, I
dc.date1999-Sep
dc.date2015-11-27T12:19:42Z
dc.date2015-11-27T12:19:42Z
dc.date.accessioned2018-03-29T00:53:45Z
dc.date.available2018-03-29T00:53:45Z
dc.identifierActa Crystallographica. Section D, Biological Crystallography. v. 55, n. Pt 9, p. 1614-5, 1999-Sep.
dc.identifier0907-4449
dc.identifier
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/10489464
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/194425
dc.identifier10489464
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1294658
dc.descriptionThe 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.
dc.description55
dc.description1614-5
dc.languageeng
dc.relationActa Crystallographica. Section D, Biological Crystallography
dc.relationActa Crystallogr. D Biol. Crystallogr.
dc.rightsaberto
dc.rights
dc.sourcePubMed
dc.subjectCatalase
dc.subjectCrystallization
dc.subjectHumans
dc.subjectPlacenta
dc.subjectPregnancy Proteins
dc.subjectX-ray Diffraction
dc.titleCrystallization And Preliminary X-ray Diffraction Studies Of Human Catalase.
dc.typeArtículos de revistas


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