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Two‐dimensional lattices of porin diffract to 6 Å resolution
Author(s) -
Büldt Georg,
Mischel Maja,
Hentschel Manfred P.,
Regenass Martin,
Rosenbusch Jürg P.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80859-6
Subject(s) - porin , diffraction , bacterial outer membrane , crystallography , membrane , integral membrane protein , resolution (logic) , membrane protein , chemistry , materials science , biophysics , escherichia coli , biology , optics , biochemistry , physics , gene , artificial intelligence , computer science
Porin (the product of gene ompF ) is an integral membrane protein ( M r 36 500) of the outer membrane of Escherichia coli (strain B E ). The protein has been purified to homogeneity and reconstituted in dimyristoyl‐lecithin. Oriented specimen on a flat surface yielded X‐ray diffraction pattern, originating from the two‐dimensional protein lattice, to a resolution reaching 6 Å. Although these powder rings are broad compared to corresponding diffraction patterns from purple membranes of Halobacterium halobium , porin is the first reconstituted integral membrane protein which shows diffraction to this resolution.