Crystallization and preliminary X-ray characterization of maltoporin from Escherichia coli |
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| Authors: | K A Stauffer M G Page A Hardmeyer T A Keller R A Pauptit |
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| Affiliation: | Department of Microbiology, University of Basel, Switzerland. |
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| 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. |
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