Purification, crystallisation and X-ray diffraction study of fully functional laccases from two ligninolytic fungi

被引:51
作者
Antorini, M
Herpoël-Gimbert, I
Choinowski, T
Sigoillot, JC
Asther, M
Winterhalter, K
Piontek, K
机构
[1] Swiss Fed Inst Technol, Swiss Fed Inst Technol, Inst Biochem, CH-8092 Zurich, Switzerland
[2] Univ Provence Mediterranee, Fac Sci Luminy, ESIL,IFR BAIM 86, INRA,Unite INRA Biotechnol Champignons Filamenteu, F-13288 Marseille, France
来源
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 2002年 / 1594卷 / 01期
关键词
laccase; micro-heterogeneity; crystal; structure; fungus;
D O I
10.1016/S0167-4838(01)00289-8
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Laccase isozymes from the white-rot basidiomycete fungi Trametes versicolor and Pycnoporus cinnabarinus were purified to apparent iso-electric homogeneity and crystallised. T versicolor laccase crystallises in two crystal forms, both with the orthorhombic space group P2(1)2(1)2(1), which diffract to 1.9 and 2.95 Angstrom resolution, respectively. The crystals of P. cinnabarinus laccase belong to the monoclinic space group C2 and diffract to at least 2.2 Angstrom resolution. All the laccase crystals are suitable for X-ray structure determination and contain a full complement of copper ions. (C) 2002 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:109 / 114
页数:6
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