The three‐dimensional structure of porin from Rhodobacter capsulatus at 3 Å resolution
- 16 July 1990
- journal article
- Published by Wiley in FEBS Letters
- Vol. 267 (2) , 268-272
- https://doi.org/10.1016/0014-5793(90)80942-c
Abstract
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.Keywords
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