PMID:8589999
| Citation |
Cowan, SW, Garavito, RM, Jansonius, JN, Jenkins, JA, Karlsson, R, König, N, Pai, EF, Pauptit, RA, Rizkallah, PJ and Rosenbusch, JP (1995) The structure of OmpF porin in a tetragonal crystal form. Structure 3:1041-50 |
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| Abstract |
OmpF porin is a trimeric integral membrane protein responsible for the passive transport of small hydrophilic molecules, such as nutrients and waste products, across the outer membrane of Escherichia coli. Very few membrane proteins have been crystallized in three dimensions, yet this stable protein can be obtained in several crystal forms. Comparison of the structures of the same membrane protein in two different packing environments is of major interest, because it allows us to explore the integrity of the structure outside the natural membrane environment. |
| Links | |
| Keywords |
Amino Acid Sequence; Bacterial Outer Membrane Proteins/chemistry; Crystallography, X-Ray/methods; Iridium/chemistry; Models, Molecular; Molecular Sequence Data; Platinum/chemistry; Protein Conformation; Protein Folding; Software; Temperature |
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