Crystallization and preliminary X-ray diffraction analysis of the small laccase from Streptomyces coelicolor

被引:14
作者
Skalova, Tereza [1 ]
Dohnalek, Jan [1 ,2 ]
Ostergaard, Lars Henrik [3 ]
Ostergaard, Peter Rahbek [3 ]
Kolenko, Petr [1 ]
Duskova, Jarmila [1 ]
Hasek, Jindrich [1 ]
机构
[1] Acad Sci Czech Republ, Inst Macromol Chem, CZ-16206 Prague, Czech Republic
[2] Acad Sci Czech Republ, Inst Phys, CZ-16253 Prague, Czech Republic
[3] Novozymes A S, DK-2880 Bagsvaerd, Denmark
来源
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2007年 / 63卷
关键词
Laccases; Multicopper blue proteins; Oxidoreductases;
D O I
10.1107/S1744309107060721
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The small bacterial laccase from the actinobacterium Streptomyces coelicolor which lacks the second of the three domains of the laccases structurally characterized to date was crystallized. This multi-copper phenol oxidase crystallizes in a primitive tetragonal lattice, with unit-cell parameters a = b = 179.8, c = 175.3 angstrom. The crystals belong to either space group P4(1)2(1)2 or P4(3)2(1)2. The self-rotation function shows the presence of a noncrystallographic threefold axis in the structure. Phases will be determined from the anomalous signal of the natively present copper ions.
引用
收藏
页码:1077 / 1079
页数:3
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