Crystallization and preliminary X-ray diffraction analysis of the small laccase from Streptomyces coelicolor.
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 A. 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.
Skálová
Tereza
T
Institute of Macromolecular Chemistry, Academy of Sciences of the Czech Republic, Heyrovského nám. 2, 162 06 Praha 6, Czech Republic. skalova@imc.cas.cz
Dohnálek
Jan
J
Ostergaard
Lars Henrik
LH
Ostergaard
Peter Rahbek
PR
Kolenko
Petr
P
Dusková
Jarmila
J
Hasek
Jindrich
J
D003460:Crystallization; D042845:Laccase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008970:Molecular Weight; D048372:Streptomyces coelicolor / Q000201:enzymology* / Q000235:genetics; D014961:X-Ray Diffraction
D042845:Laccase