1O81

Tryparedoxin II from C.fasciculata solved by sulphur phasing

Summary for 1O81

• Entry DOI: 10.2210/pdb1o81/pdb
• Descriptor: TRYPAREDOXIN II, SULFATE ION (3 entities in total)
• Functional Keywords: electron transport, tryparedoxin ii, sulphur phasing, sad, s-sad
• Biological source: CRITHIDIA FASCICULATA
• Total number of polymer chains: 2
• Total formula weight: 34423.51

Authors

Leonard, G.A.,Micossi, E.,Hunter, W.N. (deposition date: 2002-11-21, release date: 2002-12-19, Last modification date: 2019-10-09)

Primary citation

Micossi, E.,Hunter, W.N.,Leonard, G.A.
De Novo Phasing of Two Crystal Forms of Tryparedoxin II Using the Anomalous Scattering from S Atoms: A Combination of Small Signal and Medium Resolution Reveals This to be a General Tool for Solving Protein Crystal Structures
Acta Crystallogr.,Sect.D, 58:21-, 2002

PubMed Abstract: The de novo phasing of the structures of two crystal forms of tryparedoxin II from Crithidia fasciculata has been carried out using single-wavelength anomalous diffraction techniques exploiting only the small anomalous signal from the S atoms intrinsic to the native protein. Data were collected at 1.77 A wavelength, where the Bijvoet ratio is approximately 1.2%. Data collected to d(min) = 2.5 A from a crystal of form I, which has a diffraction limit of d(min) = 1.5 A and a solvent content of approximately 46%, produced readily interpretable electron-density maps. When these phases were extended to the resolution limit of the crystals, almost the entire model could be traced automatically. Crystals of form II have a much higher solvent content, approximately 72%, and a much lower diffraction limit than form I and at 1.77 A wavelength yielded data only to d(min) = 2.7 A. Despite the medium resolution of the data for this crystal form, it was possible both to determine the heavy-atom partial structure and then use it to produce, still at d(min) = 2.7 A, an excellent quality interpretable electron-density map. This was then improved by phase extension to the d(min) = 2.35 A diffraction limits of a different crystal for which data were collected on a more intense beamline. The success of this latter structure solution markedly increases the potential use in macromolecular crystal structure determination of the anomalous signal available from S atoms that occur naturally in proteins and, as is discussed, has significant implications for structure determination in the high-throughput era.

PubMed: 11752776
DOI: 10.1107/S0907444901016808

Experimental method

X-RAY DIFFRACTION (1.5 Å)