| Literature DB >> 2165921 |
M S Weiss1, T Wacker, J Weckesser, W Welte, G E Schulz.
Abstract
The crystal structure of porin from Rhodobacter capsulatus strain 37b4 has been solved at 3.0 A (1 A = 0.1 nm) resolution by multiple isomorphous replacement and solvent-flattening. The three pores of the trimer are well defined in the electron density map. Each pore consists of a 16-stranded beta-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 A by 10 A. The eye-let has an axial length of about 10 A; it defines the exclusion limit for diffusing particles.Entities:
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Year: 1990 PMID: 2165921 DOI: 10.1016/0014-5793(90)80942-c
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124