Three-dimensional crystals of an integral membrane protein: an initial x-ray analysis.
The Journal of Cell BiologyPublished 1 July 1980Open access
R. Michael Garavito, Jürg P. Rosenbusch
Citations272
SJR quartileQ1
SJR score3.36
SNIP1.52
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TL;DR
Matrix protein, a pore-forming transmembrane protein spanning the outer membrane of Escherichia coli, has been obtained in a variety of three- dimensional crystal forms amenable to both electron microscope and x- ray analyses.
Abstract
Matrix protein, a pore-forming transmembrane protein spanning the outer membrane of Escherichia coli, has been obtained in a variety of three-dimensional crystal forms amenable to both electron microscope and x-ray analyses. Successful association into large crystals depended on the use of alpha-octyl glucoside, a detergent with relatively low affinity for the protein. Electron micrographs of thin-sectioned crystals show a high degree of order. Preliminary crystallographic data suggest that the crystals, which exhibit diffraction to 3.8 A, have a cubic space group.
Keywords
Materials ScienceBiochemistry, Genetics and Molecular Biology
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