Purification and preliminary crystallographic study of Trametes versicolor laccase in its native form

被引:28
|
作者
Bertrand, T
Jolivalt, C
Caminade, E
Joly, N
Mougin, C
Briozzo, P [1 ]
机构
[1] Inst Natl Agron Paris Grignon, Chim Biol Lab, F-78850 Thiverval Grignon, France
[2] CNRS, UPR 9063, Lab Enzymol & Biochim Struct, F-91198 Gif Sur Yvette, France
[3] INRA, Lab Phytopharm & Mediateurs Chim, F-78026 Versailles, France
关键词
D O I
10.1107/S0907444901019898
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Laccases are multi-copper oxidases that catalyse the oxidation of a wide range of phenols and their use in industrial oxidative processes is increasing. A laccase has been purified from the fungus Trametes versicolor and crystallized using the hanging-drop method. Crystals belong to the monoclinic space group P2(1), with unit-cell parameters a = 87.7, b = 110.5, c = 123.2 Angstrom, beta = 103.4degrees. A complete data set was collected to 2.4 Angstrom resolution on a Cu Kalpha rotating-anode X-ray source. Molecular replacement was performed and the initial electron-density maps indicate that the four expected Cu atoms are all present.
引用
收藏
页码:319 / 321
页数:3
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