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The three‐dimensional structure of porin from Rhodobacter capsulatus at 3 Å resolution
Author(s) -
Weiss M.S.,
Wacker T.,
Weckesser J.,
Weite W.,
Schulz G.E.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80942-c
Subject(s) - rhodobacter , trimer , crystallography , porin , resolution (logic) , chemistry , barrel (horology) , flattening , photosynthetic reaction centre , geometry , materials science , electron transfer , bacterial outer membrane , mathematics , dimer , mutant , photochemistry , artificial intelligence , computer science , composite material , gene , biochemistry , organic chemistry , escherichia coli
The crystal structure of porin from Rhodobacter capsulatus strain 37b4 has been solved at 3.0 Å (1 Å = 0.1 nm) resolution by multiple isomorphous replacement and solvent‐flattening. The three pores of the trimer are well denned in the electron density map. Each pore consists of a 16‐stranded β‐barrel which traverses the membrane as a tube. Near its center the tube is narrowed by chain segments protruding from the inner wall of the barrel that form an eye‐let with an irregular cross‐section of about 6 Å by 10 Å. The eye‐let has an axial length of about 10 Å; it defines the exclusion limit for diffusing particles.