Crystals of an integral membrane protein diffracting to 1.8 A resolution.

TL;DR: The results support a topological model for glutamate receptor subunits that consists of three transmembrane domains, M1, M3, and M4, and another domain, the proposed channel-lining M2, which forms a reentrant membrane segment with both ends facing the cytoplasm.

TL;DR: A “hybrid” droplet-based microfluidic approach that combines the steps of screening and optimization into one simple experiment and uses nanoliter-sized plugs to minimize sample consumption is reported.

TL;DR: It is demonstrated that the crystallization of the cytochrome c oxidase from Paracoccus denitrificans can be mediated by co-crystallization with an antibody Fv fragment, which should be useful in obtaining well-ordered crystals of membrane proteins in general.

TL;DR: The comparison of the structures of the same membrane protein in two different packing environments reveals that the overall structure of OmpF is not influenced by crystal lattice constraints and, thus, presumably bears close resemblance to the in vivo structure.

TL;DR: 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.

TL;DR: Porin monomers of the phototrophic bacterium Rhodobacter capsulatus were purified using the vapor phase equilibration technique and Reflexions were observed to 3.2 Å.

TL;DR: Porin; Membrane protein structure; X‐ray structure; Rhodobacter capsulatus; (Rhodobacter Capsulatus) – structure and function.

TL;DR: The major outer membrane protein of Rhodobacter capsulatus 37 b4 (capsule-free) was isolated and Analytical ultracentrifugation studies demonstrated the native porin to be a trimer.