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 - Mar 25 2009
Externally publishedYes

Keywords

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

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Fingerprint Dive into the research topics of 'A rapid method for quantifying heavy atom derivatives for multiple isomorphous replacement in protein crystallography'. Together they form a unique fingerprint.

  • 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