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