Structure of porin refined at 1.8 A resolution.
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.
Weiss
M S
MS
Institut für Organische Chemie und Biochemie der Universität, Freiburg, Germany.
Schulz
G E
GE
D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism; D003902:Detergents; D006860:Hydrogen Bonding; D008024:Ligands; D008958:Models, Molecular; D008969:Molecular Sequence Data; D018272:Porins; D011487:Protein Conformation; D016354:Rhodobacter capsulatus / Q000737:chemistry; D012997:Solvents; D014961:X-Ray Diffraction
D001425:Bacterial Outer Membrane Proteins; D003902:Detergents; D008024:Ligands; D018272:Porins; D012997:Solvents; D002118:Calcium