Electron Density Profile of Two-dimensionally Crystalline Membranous Cytochrome C Oxidase at Low Resolution

Overview

Journal Biophys J

Publisher Cell Press

Specialty Biophysics

Date 1987 Mar 1

PMID 3032293

Citations 1

Authors

U Jayaraman

T Chang

T G Frey

J K Blasie

Affiliations

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Abstract

Unilamellar vesicles of membranous cytochrome c oxidase have been isolated whose distribution of protein in the membrane plane was predominantly crystalline. The vesicles were collapsed via controlled partial dehydration, resulting, at first, in the formation of unoriented, mostly unstacked, membrane pairs. Further controlled partial dehydration resulted in the formation of oriented multilayers of stacks of membrane pairs, retaining the in-plane crystallinity. The above were monitored by electron microscopy and x-ray diffraction. Analysis of the x-ray diffraction from unoriented, unstacked membrane pairs by two independent methods provided the membrane electron density profile to 30 A resolution.

Citing Articles

Moderate resolution profile structure of the sarcoplasmic reticulum membrane under low temperature conditions for the transient trapping of E1 approximately P.

Pascolini D, Blasie J Biophys J. 1988; 54(4):669-78.

PMID: 2975955 PMC: 1330371. DOI: 10.1016/S0006-3495(88)83002-9.

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