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

Publication ,  Journal Article
Frey, W; Schief, WR; Pack, DW; Chen, CT; Chilkoti, A; Stayton, P; Vogel, V; Arnold, FH
Published in: Proceedings of the National Academy of Sciences of the United States of America
May 1996

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.

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Published In

Proceedings of the National Academy of Sciences of the United States of America

DOI

EISSN

1091-6490

ISSN

0027-8424

Publication Date

May 1996

Volume

93

Issue

10

Start / End Page

4937 / 4941

Related Subject Headings

  • Surface Properties
  • Streptavidin
  • Proteins
  • Point Mutation
  • Mutagenesis, Site-Directed
  • Models, Molecular
  • Metals
  • Lipids
  • Ions
  • Histidine
 

Citation

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Frey, W., Schief, W. R., Pack, D. W., Chen, C. T., Chilkoti, A., Stayton, P., … Arnold, F. 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), 4937–4941. https://doi.org/10.1073/pnas.93.10.4937
Frey, W., W. R. Schief, D. W. Pack, C. T. Chen, A. Chilkoti, P. Stayton, V. Vogel, and F. H. Arnold. “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, no. 10 (May 1996): 4937–41. https://doi.org/10.1073/pnas.93.10.4937.
Frey W, Schief WR, Pack DW, Chen CT, Chilkoti A, Stayton P, et al. 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. 1996 May;93(10):4937–41.
Frey, W., et al. “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, vol. 93, no. 10, May 1996, pp. 4937–41. Epmc, doi:10.1073/pnas.93.10.4937.
Frey W, Schief WR, Pack DW, Chen CT, Chilkoti A, Stayton P, Vogel V, Arnold FH. 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. 1996 May;93(10):4937–4941.
Journal cover image

Published In

Proceedings of the National Academy of Sciences of the United States of America

DOI

EISSN

1091-6490

ISSN

0027-8424

Publication Date

May 1996

Volume

93

Issue

10

Start / End Page

4937 / 4941

Related Subject Headings

  • Surface Properties
  • Streptavidin
  • Proteins
  • Point Mutation
  • Mutagenesis, Site-Directed
  • Models, Molecular
  • Metals
  • Lipids
  • Ions
  • Histidine