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A rapid method for quantifying heavy atom derivatives for multiple isomorphous replacement in protein crystallography
Author(s) -
Colip Leslie A.,
Koppisch Andrew T.,
Broene Richard D.,
Berger Jennifer A.,
Baldwin Sharon M.,
Harris Michael N.,
Peterson Lori J.,
Warner Benjamin P.,
Birnbaum Eva R.
Publication year - 2009
Publication title -
journal of applied crystallography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.429
H-Index - 162
ISSN - 1600-5767
DOI - 10.1107/s0021889809000077
Subject(s) - atom (system on chip) , crystallography , chemistry , fluorescence , protein crystallization , diffraction , x ray crystallography , stoichiometry , multiple isomorphous replacement , crystal structure , crystallization , physics , computer science , organic chemistry , optics , embedded system , quantum mechanics
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.