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

doi:10.1107/S0021889809000077

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

Chemistry and Biochemistry

Research output: Contribution to journal › Article › peer-review

3 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 language	English (US)
Pages (from-to)	329-332
Number of pages	4
Journal	Journal of Applied Crystallography
Volume	42
Issue number	2
DOIs	https://doi.org/10.1107/S0021889809000077
State	Published - 2009

Keywords

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

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology

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10.1107/S0021889809000077

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title = "A rapid method for quantifying heavy atom derivatives for multiple isomorphous replacement in protein crystallography",

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.",

keywords = "Heavy atom derivatization, Multiple isomorphous replacement, Protein crystallography, X-ray fluorescence",

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

year = "2009",

doi = "10.1107/S0021889809000077",

language = "English (US)",

volume = "42",

pages = "329--332",

journal = "Journal of Applied Crystallography",

issn = "0021-8898",

publisher = "International Union of Crystallography",

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TY - JOUR

T1 - A rapid method for quantifying heavy atom derivatives for multiple isomorphous replacement in protein crystallography

AU - Colip, Leslie A.

AU - Koppisch, Andrew T.

AU - Broene, Richard D.

AU - Berger, Jennifer A.

AU - Baldwin, Sharon M.

AU - Harris, Michael N.

AU - Peterson, Lori J.

AU - Warner, Benjamin P.

AU - Birnbaum, Eva R.

PY - 2009

Y1 - 2009

N2 - 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.

AB - 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.

KW - Heavy atom derivatization

KW - Multiple isomorphous replacement

KW - Protein crystallography

KW - X-ray fluorescence

UR - https://www.scopus.com/pages/publications/62649141872

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DO - 10.1107/S0021889809000077

M3 - Article

AN - SCOPUS:62649141872

SN - 0021-8898

VL - 42

SP - 329

EP - 332

JO - Journal of Applied Crystallography

JF - Journal of Applied Crystallography

IS - 2

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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