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Two-dimensional protein crystallization via metal-ion coordination by naturally occurring surface histidines

Frey, Wolfgang and Schief, William R., Jr. and Pack, Daniel W. and Chen, Chao-Tsen and Chilkoti, Ashutosh and Stayton, Patrick and Vogel, Viola and Arnold, Frances H. (1996) Two-dimensional protein crystallization via metal-ion coordination by naturally occurring surface histidines. Proceedings of the National Academy of Sciences of the United States of America, 93 (10). pp. 4937-4941. ISSN 0027-8424. http://resolver.caltech.edu/CaltechAUTHORS:FREpnas96

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Abstract

A powerful and potentially general approach to the targeting and crystallization of proteins on lipid interfaces through coordination of surface histidine residues to lipid-chelated divalent metal ions is presented. This approach, which should be applicable to the crystallization of a wide range of naturally occurring or engineered proteins, is illustrated here by the crystallization of streptavidin on a monolayer of an iminodiacetate-Cu(II) lipid spread at the air-water interface. This method allows control of the protein orientation at interfaces, which is significant for the facile production of highly ordered protein arrays and for electron density mapping in structural analysis of two-dimensional crystals. Binding of native streptavidin to the iminodiacetate-Cu lipids occurs via His-87, located on the protein surface near the biotin binding pocket. The two-dimensional streptavidin crystals show a previously undescribed microscopic shape that differs from that of crystals formed beneath biotinylated lipids.


Item Type:Article
Additional Information:© 1996 by The National Academy of Sciences Communicated by Charles R. Cantor, Boston University, Boston, MA, December 28, 1995 (received for review November 13, 1995) W.F. was supported by a Feodor-Lynen fellowship from the Alexander von Humboldt Foundation, W.R.S. by a Biotechnology training grant fellowship from the National Institutes of Health (GM 08437), and D.W.P. by a training fellowship from the National Institute of General Medical Sciences (National Research Service Award 1 T32 GM 08346-01). This research was supported by the National Aeronautics and Space Administration (NAG 8-1149), the Office of Naval Research (N00014-92-J-1178), and the U.S. Army Research Office. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.
Record Number:CaltechAUTHORS:FREpnas96
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:FREpnas96
Alternative URL:http://www.pnas.org/cgi/content/abstract/93/10/4937
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:643
Collection:CaltechAUTHORS
Deposited By: Archive Administrator
Deposited On:09 Sep 2005
Last Modified:14 Nov 2014 19:18

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