Structure of porin refined at 1.8 A resolution.

M S Weiss, G E Schulz
Author Information
  1. M S Weiss: Institut für Organische Chemie und Biochemie der Universität, Freiburg, Germany.

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.

MeSH Term

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

Chemicals

Bacterial Outer Membrane Proteins
Detergents
Ligands
Porins
Solvents
Calcium

Word Cloud

Created with Highcharts 10.0.0porinrefinedfinalmodelthreemoleculesdetergentresolution18crystalstructureRhodobactercapsulatususingsimulatedannealingmethodconsists301aminoacidresidueswellobeyingstandardgeometrycalciumions274solventoneunknownligandmodeledmoleculecrystallographicR-factor186%based42851independentreflectionsrange10describeddetailStructure

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