help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS

Biophysical Journal 61: 172-188 (1992)
© 1992 the Biophysical Society

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Paul, A
Right arrow Articles by Baumeister, W
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Paul, A
Right arrow Articles by Baumeister, W

Two-dimensional crystallization of a bacterial surface protein on lipid vesicles under controlled conditions.

A Paul, H Engelhardt, U Jakubowski and W Baumeister

Max-Planck-Institut für Biochemie, Martinsried, Germany.

ABSTRACT

The solubilized surface protein of the Gram-negative bacterium Comamonas acidovorans was reconstituted on lipid vesicles by means of controlled dialysis. To this end, a multichamber dialysis apparatus was built which allows one to control the temperature and the dialysis rate, to apply various temperatures or buffer systems and sample conditions in a single experiment, and to monitor the turbidity of the sample by means of light scattering. The reconstitution conditions were optimized such that the surface protein formed two-dimensional crystals suitable for electron crystallography. The recrystallized surface protein arrays gave a resolution of approximately 1.3 nm in projection after correlation averaging of negatively stained preparations. The surface protein assembled into partially self-contained two-dimensional crystals which possess a strong shape-determining effect and formed cylinders and various cone-shaped vesicles. The development of the various vesicle forms is described in a model.




This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
H. Engelhardt, C. Heinz, and M. Niederweis
A Tetrameric Porin Limits the Cell Wall Permeability of Mycobacterium smegmatis
J. Biol. Chem., September 27, 2002; 277(40): 37567 - 37572.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Pajatsch, C. Andersen, A. Mathes, A. Bock, R. Benz, and H. Engelhardt
Properties of a Cyclodextrin-specific, Unusual Porin from Klebsiella oxytoca
J. Biol. Chem., August 27, 1999; 274(35): 25159 - 25166.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1992 by the Biophysical Society.