A complement to the modern crystallographer's toolbox: caged gadolinium complexes with versatile binding modes. (1st June 2014)

• Record Type: Journal Article
• Authors: Stelter, Meike; Molina, Rafael; Jeudy, Sandra; Kahn, Richard; Abergel, Chantal; Hermoso, Juan A.
• Is Part Of: Acta crystallographica. Volume 70:Part 6(2014:Jun.)
• Page Start: 1506
• Page End: 1516
• Publication Date: 2014-06-01
• Subjects: Biomolecules -- Structure -- Periodicals; Physical biochemistry -- Periodicals; X-ray crystallography -- Periodicals; Crystallography -- Periodicals; 572
• DOI: 10.1107/S1399004714005483
• Languages: English
• ISSNs: 0907-4449

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>A set of seven caged gadolinium complexes were used as vectors for introducing the chelated Gd³⁺ ion into protein crystals in order to provide strong anomalous scattering for <italic>de novo</italic> phasing. The complexes contained multidentate ligand molecules with different functional groups to provide a panel of possible interactions with the protein. An exhaustive crystallographic analysis showed them to be nondisruptive to the diffraction quality of the prepared derivative crystals, and as many as 50% of the derivatives allowed the determination of accurate phases, leading to high‐quality experimental electron‐density maps. At least two successful derivatives were identified for all tested proteins. Structure refinement showed that the complexes bind to the protein surface or solvent‐accessible cavities, involving hydrogen bonds, electrostatic and CH–π interactions, explaining their versatile binding modes. Their high phasing power, complementary binding modes and ease of use make them highly suitable as a heavy‐atom screen for high‐throughput <italic>de novo</italic> structure determination, in combination with the SAD method. They can also provide a reliable tool for the development of new methods such as serial femtosecond crystallography.</p> </abstract>