Structure of porin refined at 1.8 A resolution

J Mol Biol. 1992 Sep 20;227(2):493-509. doi: 10.1016/0022-2836(92)90903-w.

Abstract

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 A. The model is described in detail.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Outer Membrane Proteins / chemistry*
  • Bacterial Outer Membrane Proteins / metabolism
  • Binding Sites
  • Calcium / metabolism
  • Detergents
  • Hydrogen Bonding
  • Ligands
  • Models, Molecular
  • Molecular Sequence Data
  • Porins
  • Protein Conformation
  • Rhodobacter capsulatus / chemistry
  • Solvents
  • X-Ray Diffraction

Substances

  • Bacterial Outer Membrane Proteins
  • Detergents
  • Ligands
  • Porins
  • Solvents
  • Calcium