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© Institut Pasteur
Cells infected for 24 hrs with C. Trachomatis. The cell nuclei are labelled in blue, the bacteria appear yellow, within the inclusion lumen. A bacterial protein secreted out the inclusion into the host cytoplasm id labelled in red.
Publication : Acta crystallographica. Section D, Biological crystallography

Advantages of high-resolution phasing: MAD to atomic resolution

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Acta crystallographica. Section D, Biological crystallography - 23 Aug 2002

Schmidt A, Gonzalez A, Morris RJ, Costabel M, Alzari PM, Lamzin VS

Link to Pubmed [PMID] – 12198299

Acta Crystallogr. D Biol. Crystallogr. 2002 Sep;58(Pt 9):1433-41

The structure of the endoglucanase A from Clostridium thermocellum CelA was re-solved by three-wavelength MAD. Experimental phases were obtained in the resolution range 25-1.0 A. Various structure-solution approaches were tested in order to quantify the contribution of each wavelength. Two-wavelength MAD phasing was sufficient to obtain excellent experimental phases. SAD at the remote wavelength also resulted in interpretable maps. The three-wavelength MAD electron-density map was of excellent quality: for parts of the structure, atom types and bond types could be easily assigned. Double bonds in peptide links and side chains could be located owing to their increased electron density indicating their pi character. Comparison with a previously determined structure of CelA at 1.65 A showed that, apart from a few additional multiple conformers and differently oriented side chains, major differences occur at the protein-solvent interface. A complete additional solvent shell could be observed and the inner shells have been completed. The high accuracy of the structure allowed unambiguous assignment of the protonation state for the active-site catalytic carboxylates.

http://www.ncbi.nlm.nih.gov/pubmed/12198299