A rapid method for quantifying heavy atom derivatives for multiple isomorphous replacement in protein crystallography

Leslie A. Colip, Andrew T Koppisch, Richard D. Broene, Jennifer A. Berger, Sharon M. Baldwin, Michael N. Harris, Lori J. Peterson, Benjamin P. Warner, Eva R. Birnbaum

Research output: Contribution to journalArticle

2 Scopus citations

Abstract

A rapid and simple X-ray fluorescence-based method is reported for characterizing heavy atom derivatives of proteins for protein crystallography using multiple isomorphous replacement (MIR). MIR is a widely used technique for solving protein crystallographic structures which requires that a 'heavy atom' be incorporated into the protein to provide a strong signal in the diffraction pattern. Current methods for determining the effectiveness of these protein-heavy atom reactions are not always successful. In contrast, X-ray fluorescence quickly determines the presence of heavy atom modifications of proteins and the stoichiometry of these modifications.

Original languageEnglish (US)
Pages (from-to)329-332
Number of pages4
JournalJournal of Applied Crystallography
Volume42
Issue number2
DOIs
StatePublished - 2009
Externally publishedYes

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Keywords

  • Heavy atom derivatization
  • Multiple isomorphous replacement
  • Protein crystallography
  • X-ray fluorescence

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Colip, L. A., Koppisch, A. T., Broene, R. D., Berger, J. A., Baldwin, S. M., Harris, M. N., Peterson, L. J., Warner, B. P., & Birnbaum, E. R. (2009). A rapid method for quantifying heavy atom derivatives for multiple isomorphous replacement in protein crystallography. Journal of Applied Crystallography, 42(2), 329-332. https://doi.org/10.1107/S0021889809000077