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OmpF porin, an integral membrane protein that serves as a passive pore for the passage of small hydrophilic molecules across the outer membrane of Escherichia coli, has been shown to have virtually identical structures in two completely different (trigonal and tetragonal) crystal forms. OmpF protein is one of the best studied membrane proteins up to now. The mature protein is comprised of 340 amino acids, and forms aqueous, voltage-gated channels that span the outer membrane and allow the diffusion of small polar molecules.