## Abstract The crystal structure of calmodulin (CaM; __M__~r~ 16, 700, 148 residues) from the ciliated protozoan __Paramecium tetraurelia__ (PCaM) has been determined and refined using 1.8 Å resolution area detector data. The crystals are triclinic, space group P1, __a__ = 29.66, __b__ = 53.79, __
Structure of native laccase from Trametes hirsuta at 1.8 Å resolution
✍ Scribed by Polyakov, Konstantin M. ;Fedorova, Tatyana V. ;Stepanova, Elena V. ;Cherkashin, Evgeny A. ;Kurzeev, Sergei A. ;Strokopytov, Boris V. ;Lamzin, Victor S. ;Koroleva, Olga V.
- Publisher
- International Union of Crystallography
- Year
- 2009
- Tongue
- English
- Weight
- 955 KB
- Volume
- 65
- Category
- Article
- ISSN
- 0907-4449
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✦ Synopsis
This paper describes the structural analysis of the native form of laccase from Trametes hirsuta at 1.8 A ˚resolution. This structure provides a basis for the elucidation of the mechanism of catalytic action of these ubiquitous proteins. The 1.8 A resolution native structure provided a good level of structural detail compared with many previously reported laccase structures. A brief comparison with the active sites of other laccases is given.
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