A complement to the modern crystallographer's toolbox: caged gadolinium complexes with versatile binding modes

Research output: Contribution to journalJournal articleResearchpeer-review

  • Meike Stelter
  • Molina, Rafael
  • Sandra Jeudy
  • Richard Kahn
  • Chantal Abergel
  • Juan A Hermoso

A set of seven caged gadolinium complexes were used as vectors for introducing the chelated Gd(3+) ion into protein crystals in order to provide strong anomalous scattering for de novo 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 de novo 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.

Original languageEnglish
JournalActa crystallographica. Section D, Biological crystallography
Volume70
Issue numberPt 6
Pages (from-to)1506-16
Number of pages11
ISSN2059-7983
DOIs
Publication statusPublished - Jun 2014

    Research areas

  • Binding Sites, Crystallography, X-Ray/methods, Gadolinium/chemistry, Molecular Structure

ID: 203019446