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Issue 11, 2017
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Principles and methods used to grow and optimize crystals of protein–metallodrug adducts, to determine metal binding sites and to assign metal ligands

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Abstract

The characterization of the interactions between biological macromolecules (proteins and nucleic acids) and metal-based drugs is a fundamental prerequisite for understanding their mechanisms of action. X-ray crystallography enables the structural analysis of such complexes with atomic level detail. However, this approach requires the preparation of highly diffracting single crystals, the measurement of diffraction patterns and the structural analysis and interpretation of macromolecule–metal interactions from electron density maps. In this review, we describe principles and methods used to grow and optimize crystals of protein–metallodrug adducts, to determine metal binding sites and to assign and validate metal ligands. Examples from the literature and experience in our own laboratory are provided and key challenges are described, notably crystallization and molecular model refinement against the X-ray diffraction data.

Graphical abstract: Principles and methods used to grow and optimize crystals of protein–metallodrug adducts, to determine metal binding sites and to assign metal ligands

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Publication details

The article was received on 27 Jul 2017, accepted on 06 Sep 2017 and first published on 20 Sep 2017


Article type: Tutorial Review
DOI: 10.1039/C7MT00219J
Citation: Metallomics, 2017,9, 1534-1547
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    Principles and methods used to grow and optimize crystals of protein–metallodrug adducts, to determine metal binding sites and to assign metal ligands

    I. Russo Krauss, G. Ferraro, A. Pica, J. A. Márquez, J. R. Helliwell and A. Merlino, Metallomics, 2017, 9, 1534
    DOI: 10.1039/C7MT00219J

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