ArticleActa crystallographica. Section D, Biological crystallography2010
The magic triangle goes MAD: experimental phasing with a bromine derivative.
Article in Acta crystallographica. Section D, Biological crystallography, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Specific radiation damage to halogenated inhibitors and ligands in protein-ligand crystal structures.Journal of applied crystallography · 2024Article
- MicroED in drug discovery.Current opinion in structural biology · 2023Review
- Heavy Atom Detergent/Lipid Combined X-ray Crystallography for Elucidating the Structure-Function Relationships of Membrane Proteins.Membranes · 2021Review
- Simplified heavy-atom derivatization of protein structures via co-crystallization with the MAD tetragon tetrabromoterephthalic acid.Acta crystallographica. Section F, Structural biology communications · 2021Article
- An overview of heavy-atom derivatization of protein crystals.Acta crystallographica. Section D, Structural biology · 2016Review
- The Halogen Bond.Chemical reviews · 2016Review
- Crystal structure of a lipoxygenase from Cyanothece sp. may reveal novel features for substrate acquisition.Journal of lipid research · 2016Article
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- Crystallization and preliminary X-ray diffraction analysis of full-length spr1814, a response regulator of Streptococcus pneumoniae, in complex with a phosphoryl analogue.Acta crystallographica. Section F, Structural biology communications · 2014Article
- A rapid and rational approach to generating isomorphous heavy-atom phasing derivatives.The FEBS journal · 2014Article
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Authors and funding
3 authors.
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Abstract
Experimental phasing is an essential technique for the solution of macromolecular structures. Since many heavy-atom ion soaks suffer from nonspecific binding, a novel class of compounds has been developed that combines heavy atoms with functional groups for binding to proteins. The phasing tool 5-amino-2,4,6-tribromoisophthalic acid (B3C) contains three functional groups (two carboxylate groups and one amino group) that interact with proteins via hydrogen bonds. Three Br atoms suitable for anomalous dispersion phasing are arranged in an equilateral triangle and are thus readily identified in the heavy-atom substructure. B3C was incorporated into proteinase K and a multiwavelength anomalous dispersion (MAD) experiment at the Br K edge was successfully carried out. Radiation damage to the bromine-carbon bond was investigated. A comparison with the phasing tool I3C that contains three I atoms for single-wavelength anomalous dispersion (SAD) phasing was also carried out.
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