STRUCTURE OF ANIONIC SALMON TRYPSIN IN A 2ND CRYSTAL FORM

被引:11
作者
BERGLUND, GI
SMALAS, AO
HORDVIK, A
机构
[1] UNIV TROMSO,INST MATH & PHYS SCI,DEPT CHEM,PROT CRYSTALLOG GRP,N-9037 TROMSO,NORWAY
[2] UNIV TROMSO,INST MED BIOL,DEPT BIOTECHNOL,N-9037 TROMSO,NORWAY
来源
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1995年 / 51卷
关键词
D O I
10.1107/S0907444995000333
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Anionic salmon trypsin in a second crystal form (ST-IIB) has been refined at 1.83 Angstrom resolution. The crystals are orthorhombic and belong to space group P2(1)2(1)2 with lattice parameters a = 77.09, b = 82.33 and c = 31.16 Angstrom. The present structure has been compared to salmon trypsin as it appears in a previously reported crystal form (ST-IIA) with cell dimensions a = 61.95, b = 84.33 and c = 39.11 Angstrom [Smalas & Hordvik (1993). Acta Cryst. D49, 318-330]. The presence of a sulfate group involved in several hydrogen bonds to active-site residues, and the location of an additional benzamidine site in the crystal lattice, are the most striking differences between the present and the previous structure. Superposition of main-chain atoms in the two structures give an overall r.m.s. difference of 0.26 Angstrom, with the main differences located to areas with different molecular packing. The overall coordinate error is estimated to be between 0.20 and 0.25 Angstrom by the method of Luzzati.
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页码:725 / 730
页数:6
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