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Location-specific quantification of protein-bound metal ions by X-ray anomalous dispersion: Q-XAD
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Structural Biology. Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.ORCID iD: 0000-0003-3686-3062
Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.ORCID iD: 0000-0001-5574-9383
2019 (English)In: Acta Crystallographica Section D: Structural Biology, ISSN 2059-7983, Vol. 75, no 8, p. 764-771Article in journal (Refereed) Published
Abstract [en]

Here, a method is described which exploits X-ray anomalous dispersion (XAD) to quantify mixtures of metal ions in the binding sites of proteins and can be applied to metalloprotein crystals of average quality. This method has successfully been used to study site-specific metal binding in a protein from the R2-like ligand-binding oxidase family which assembles a hetero­dinuclear Mn/Fe cofactor. While previously only the relative contents of Fe and Mn in each metal-binding site have been assessed, here it is shown that the method can be extended to quantify the relative occupancies of at least three different transition metals, enabling complex competition experiments. The number of different metal ions that can be quantified is only limited by the number of high-quality anomalous data sets that can be obtained from one crystal, as one data set has to be collected for each transition-metal ion that is present (or is suspected to be present) in the protein, ideally at the absorption edge of each metal. A detailed description of the method, Q-XAD, is provided.

Place, publisher, year, edition, pages
2019. Vol. 75, no 8, p. 764-771
Keywords [en]
metal quantification, quantitative X-ray anomalous dispersion, R2-like ligand-binding oxidase, Q-XAD, X-ray crystallography
National Category
Structural Biology
Research subject
Biology with specialization in Structural Biology
Identifiers
URN: urn:nbn:se:uu:diva-389995DOI: 10.1107/S2059798319009926ISI: 000478721300006PubMedID: 31373575OAI: oai:DiVA.org:uu-389995DiVA, id: diva2:1340146
Funder
Swedish Research Council, 2016-03770Swedish Research Council, 2017-04018EU, European Research Council, HIGH-GEAR 724394Knut and Alice Wallenberg Foundation, 2012.0233Knut and Alice Wallenberg Foundation, 2017.0275EU, FP7, Seventh Framework Programme, 283570Available from: 2019-08-02 Created: 2019-08-02 Last updated: 2019-09-27Bibliographically approved

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