The stalks (hyphae) of a prosthecate bacterium, directly sampled from the water surface of a hot pond, show extended regular patterns on their envelope in the electron microscope. Image processing revealed a structure of the crystalline complexes which is very similar to the gross morphology of the Escherichia coli porins OmpC and OmpF. The natural two-dimensional crystal of the outer membrane protein has p3 symmetry and a lattice constant of 7.95 nm. The three-dimensional structure of the stalk porin has been determined to an almost isotropic resolution of 1.7 nm. The reconstruction revealed a complex network of channels within the membrane matrix with a triplet of pores merging into a common outlet, similar to the structure of the E. coli...
AbstractThe structure of the porin from Rhodobacter capsulanus was determined at a resolution of 1.8...
The outer membranes (OM) of many Gram-negative bacteria contain general porins, which form nonspecif...
The outer membranes (OM) of many Gram-negative bacteria contain general porins, which form nonspecif...
The stalks (hyphae) of a prosthecate bacterium, directly sampled from the water surface of a hot pon...
The stalks (hyphae) of a prosthecate bacterium, directly sampled from the water surface of a hot pon...
Porins, the major proteins found in the bacterial outer membrane, exhibit an unusual hollow β-barrel...
A single-projection structure analysis of a bacterial outer membrane protein, OmpC, has been carried...
The Escherichia coli porin OmpG, which acts as an efficient unspecific channel for mono-, di- and tr...
AbstractThe crystal structure of porin from Rhodobacter capsulatus strain 37b4 has been solved at 3....
AbstractThe crystal electron density map of porin from Rhodobacter capsulatus 37b4 at 0.6 nm resolut...
AbstractPorin (the product of gene ompF) is an integral membrane protein (Mr 36 500) of the outer me...
OmpG, a monomeric pore-forming protein from Escherichia coli outer membranes, was refolded from incl...
International audienceSummary The outer membrane of Gram-negative bacteria protects the cell against...
International audienceSummary The outer membrane of Gram-negative bacteria protects the cell against...
International audienceSummary The outer membrane of Gram-negative bacteria protects the cell against...
AbstractThe structure of the porin from Rhodobacter capsulanus was determined at a resolution of 1.8...
The outer membranes (OM) of many Gram-negative bacteria contain general porins, which form nonspecif...
The outer membranes (OM) of many Gram-negative bacteria contain general porins, which form nonspecif...
The stalks (hyphae) of a prosthecate bacterium, directly sampled from the water surface of a hot pon...
The stalks (hyphae) of a prosthecate bacterium, directly sampled from the water surface of a hot pon...
Porins, the major proteins found in the bacterial outer membrane, exhibit an unusual hollow β-barrel...
A single-projection structure analysis of a bacterial outer membrane protein, OmpC, has been carried...
The Escherichia coli porin OmpG, which acts as an efficient unspecific channel for mono-, di- and tr...
AbstractThe crystal structure of porin from Rhodobacter capsulatus strain 37b4 has been solved at 3....
AbstractThe crystal electron density map of porin from Rhodobacter capsulatus 37b4 at 0.6 nm resolut...
AbstractPorin (the product of gene ompF) is an integral membrane protein (Mr 36 500) of the outer me...
OmpG, a monomeric pore-forming protein from Escherichia coli outer membranes, was refolded from incl...
International audienceSummary The outer membrane of Gram-negative bacteria protects the cell against...
International audienceSummary The outer membrane of Gram-negative bacteria protects the cell against...
International audienceSummary The outer membrane of Gram-negative bacteria protects the cell against...
AbstractThe structure of the porin from Rhodobacter capsulanus was determined at a resolution of 1.8...
The outer membranes (OM) of many Gram-negative bacteria contain general porins, which form nonspecif...
The outer membranes (OM) of many Gram-negative bacteria contain general porins, which form nonspecif...