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

Published

Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Frey, W; Schief, WR; Pack, DW; Chen, CT; Chilkoti, A; Stayton, P; Vogel, V; Arnold, FH

Published Date

  • May 1996

Published In

Volume / Issue

  • 93 / 10

Start / End Page

  • 4937 - 4941

PubMed ID

  • 8643507

Pubmed Central ID

  • 8643507

Electronic International Standard Serial Number (EISSN)

  • 1091-6490

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.93.10.4937

Language

  • eng