ISSN:
1399-0047
Quelle:
Crystallography Journals Online : IUCR Backfile Archive 1948-2001
Thema:
Chemie und Pharmazie
,
Geologie und Paläontologie
,
Physik
Notizen:
Catalase (E.C. 1.11.1.6) was purified from human erythrocytes and crystallized in three different forms: orthorhombic, hexagonal and tetragonal. The structure of the orthorhombic crystal form of human erythrocyte catalase (HEC), with space group P212121 and unit-cell parameters a = 84.9, b = 141.7, c = 232.5 Å, was determined and refined with 2.75 Å resolution data. Non-crystallographic symmetry restraints were employed and the resulting R value and Rfree were 0.206 and 0.272, respectively. The overall structure and arrangement of HEC molecules in the orthorhombic unit cell were very similar to those of bovine liver catalase (BLC). However, no NADPH was observed in the HEC crystal and a water was bound to the active-site residue His75. Conserved lattice interactions suggested a common growth mechanism for the orthorhombic crystals of HEC and BLC.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1107/S0907444999015930
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