title: Crystallization and preliminary X-ray characterization of maltoporin from Escherichia coli.
abstract: Crystals of maltoporin (the bacteriophage lambda receptor of Escherichia coli) that diffract X-rays to 3 A resolution can be grown reproducibly. Maltoporin is an integral membrane protein, which forms a channel in the E. coli outer membrane that specifically facilitates the diffusion of maltose and maltodextrins. The crystals have a rhombic prismatic habit and belong to the orthorhombic space group C222(1) with unit cell dimensions a = 130 A, b = 213 A and c = 216 A. X-ray structure determination is underway.
authors: Department of Microbiology, University of Basel, Switzerland.
authors: K A
authors: KA
authors: Stauffer
authors: M G
authors: MG
authors: Page
authors: A
authors: A
authors: Hardmeyer
authors: T A
authors: TA
authors: Keller
authors: R A
authors: RA
authors: Pauptit
mesh_terms: D001425:Bacterial Outer Membrane Proteins; D010582:Bacteriophage lambda / Q000378:metabolism; D002458:Cell Fractionation; D002462:Cell Membrane / Q000032:analysis / Q000648:ultrastructure; D003460:Crystallization; D004926:Escherichia coli / Q000378:metabolism*; D018272:Porins; D011991:Receptors, Virus / Q000302:isolation & purification; D014961:X-Ray Diffraction
chemical_list: D001425:Bacterial Outer Membrane Proteins; D018272:Porins; D011991:Receptors, Virus; C016532:maltoporins