STRUCTURE OF PORIN REFINED AT 1.8 ANGSTROM RESOLUTION

被引：282

作者：

WEISS, MS

SCHULZ, GE

机构：

[1] Institut für Organische Chemie, Biochemie der Universität, D-7800 Freiburg im Breisgau

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1992年 / 227卷 / 02期

关键词：

PORIN; MEMBRANE CHANNEL; X-RAY DIFFRACTION; RHODOBACTER-CAPSULATUS;

D O I：

10.1016/0022-2836(92)90903-W

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：

The crystal structure of porin from Rhodobacter capsulatus has been refined using the simulated annealing method. The final model consists of all 301 amino acid residues well obeying standard geometry, three calcium ions, 274 solvent molecules, three detergent molecules and one unknown ligand modeled as a detergent molecule. The final crystallographic R-factor is 18.6% based on 42,851 independent reflections in the resolution range 10 to 1.8 Å. The model is described in detail. © 1992.

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页码：493 / 509

页数：17

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