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From Proteopedia
crystal structure of the essential E. coli YeaZ protein by MAD method using the gadolinium complex "DOTMA"
Structural highlights
Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedA 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-pi 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. A complement to the modern crystallographer's toolbox: caged gadolinium complexes with versatile binding modes.,Stelter M, Molina R, Jeudy S, Kahn R, Abergel C, Hermoso JA Acta Crystallogr D Biol Crystallogr. 2014 Jun;70(Pt 6):1506-16. doi:, 10.1107/S1399004714005483. Epub 2014 May 23. PMID:24914962[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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