title: The projection structure of microsomal glutathione transferase.
abstract: Through the use of electron crystallography, it has been possible to obtain high resolution structural information regarding a mammalian protein that spans the lipid bilayer. Two-dimensional crystals of the detoxification enzyme microsomal glutathione transferase were induced by slow detergent removal from a mixture containing low amounts of phospholipid. Images of specimens stabilized in tannin were collected using electron cryomicroscopy. The projection structure at 4 A shows tightly packed trimers of the protein. Each of them contains an inner core of six parallel alpha-helices delineating a central low density region. The helical bundle is partly surrounded by elongated domains.
authors.affiliation: Center for Structural Biochemistry, Karolinska Institutet, Novum, Huddinge, Sweden.
authors.forename: H
authors.initials: H
authors.lastname: Hebert
authors.forename: I
authors.initials: I
authors.lastname: Schmidt-Krey
authors.forename: R
authors.initials: R
authors.lastname: Morgenstern
mesh_terms: D000818:Animals; D003460:Crystallization; D003461:Crystallography / Q000379:methods; D005583:Fourier Analysis; D005982:Glutathione Transferase / Q000737:chemistry*; D008051:Lipid Bilayers; D008854:Microscopy, Electron / Q000379:methods; D008862:Microsomes, Liver / Q000201:enzymology*; D017433:Protein Structure, Secondary; D051381:Rats
chemical_list: D008051:Lipid Bilayers; D005982:Glutathione Transferase