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Open AccessJournal ArticleDOI

Three-dimensional crystals of an integral membrane protein: an initial x-ray analysis.

R M Garavito, +1 more
- 01 Jul 1980 - 
- Vol. 86, Iss: 1, pp 327-329
TLDR
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.

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Journal ArticleDOI

Analysis of membrane and surface protein sequences with the hydrophobic moment plot.

TL;DR: An algorithm has been developed which identifies alpha-helices involved in the interactions of membrane proteins with lipid bilayers and which distinguishes them from helices in soluble proteins, and suggests four transmembrane helices and a surface-seeking helix in fragment B, the moiety known to have trans Membrane function.
Journal ArticleDOI

Crystal structures explain functional properties of two E. coli porins

TL;DR: The crystal structures of matrix porin and phosphoporin both reveal trimers of identical subunits, each subunit consisting of a 16-stranded anti-parallel β-barrel containing a pore.
Journal ArticleDOI

Structure and function of bacterial outer membrane proteins: barrels in a nutshell

TL;DR: The outer membrane protects Gram‐negative bacteria against a harsh environment and the embedded proteins fulfil a number of tasks that are crucial to the bacterial cell, such as solute and protein translocation, as well as signal transduction.
Journal ArticleDOI

Interaction of membrane proteins and lipids with solubilizing detergents.

TL;DR: The nature of detergent binding by the membrane from a noncooperative to a cooperative interaction already below the critical micellar concentration is considered and it is concluded that in general binding as a monolayer ring, rather than as a micelle, is the most probable mechanism.
References
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Journal ArticleDOI

Solvent content of protein crystals.

TL;DR: An analysis of the solvent content of 116 different crystal forms of globular proteins found that in many cases this range will be sufficiently restrictive to enable the probable number of molecules in the crystallographic asymmetric unit to be determined directly from the molecular weight of the protein and the space group and unit cell dimensions of the crystal.
Journal ArticleDOI

Three-dimensional model of purple membrane obtained by electron microscopy

TL;DR: A 7-Å resolution map of the purple membrane has been obtained by electron microscopy of tilted, unstained specimens and shows that Lipid bilayer regions fill the spaces between the protein molecules.
Journal ArticleDOI

Characterization of the Major Envelope Protein from Escherichia coli REGULAR ARRANGEMENT ON THE PEPTIDOGLYCAN AND UNUSUAL DODECYL SULFATE BINDING

TL;DR: The major envelope protein from Escherichia coli has been purified by differential heat extraction in dodecyl sulfate and subsequently freed of the detergent, and its molecular weight agrees with that derived from the mobility of the major band observed in standard dodecYL sulfate gel electrophoretic analysis of unfractionated cell envelopes after treatment at 100°.
Book ChapterDOI

Properties of detergents.

TL;DR: The properties of detergents that have been used for solubilization of membranes and as a solvent medium for membrane proteins are summarized and some facts relevant to the choice of deterGents for particular experiments are presented.
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