English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  Characterization and crystal packing of three-dimensional bacteriorhodopsin crystals

Michel, H. (1982). Characterization and crystal packing of three-dimensional bacteriorhodopsin crystals. The EMBO Journal, 1(10), 1267-1271. doi:10.1002/j.1460-2075.1982.tb00023.x.

Item is

Basic

show hide
Genre: Journal Article

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Michel, Hartmut1, Author              
Affiliations:
1Max Planck Institute of Biochemistry, Max Planck Society, ou_1565141              

Content

show
hide
Free keywords: crystallization; X-ray; membrane protein; purple membrane; bacteriorhodopsin
 Abstract: The three-dimensional crystals of the integral membrane protein bacteriorhodopsin have been characterized by X-ray diffraction and freeze-fracture electron microscopy: the needle-like form A crystals belong to space group P 1 (pseudohexagonal) with seven molecules per crystallographic unit cell forming one turn of a non-crystallographic helix. The probable arrangement of the bacteriorhodopsin molecules is derived from freeze-fracture electron micrographs and chromophore orientation. Membrane-like structures are not present. The same helices of bacteriorhodopsin molecules found in crystal form A also make up the cube-like crystal form B. They are now arranged in all three mutually perpendicular directions. These cubes are always highly disordered, since the unit cell length corresponds to 6.7 molecules of the 7-fold helix. Very often, conversion of bacteriorhodopsin from the three-dimensional crystals into filamentous material occurs

Details

show
hide
Language(s): eng - English
 Dates: 1982-09-061982-10-01
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: The EMBO Journal
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Nature Publishing Group
Pages: - Volume / Issue: 1 (10) Sequence Number: - Start / End Page: 1267 - 1271 Identifier: ISSN: 0261-4189
CoNE: https://pure.mpg.de/cone/journals/resource/954925497061_1