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1a8z
From Proteopedia
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STRUCTURE DETERMINATION OF A 16.8KDA COPPER PROTEIN RUSTICYANIN AT 2.1A RESOLUTION USING ANOMALOUS SCATTERING DATA WITH DIRECT METHODS
Overview
The structure of rusticyanin, an acid-stable copper protein, has been, determined at 2.1 A resolution by direct methods combined with the, single-wavelength anomalous scattering (SAS) of copper (f" = 3.9 e-) and, then conventionally refined (Rcryst = 18.7%, Rfree = 21.9%). This is the, largest unknown protein structure (Mr approximately /= 16.8 kDa) to be, determined using the SAS and direct-methods approach and demonstrates that, by exploiting the anomalous signal at a single wavelength, direct methods, can be used to determine phases at typical (approximately 2 A), macromolecular crystallographic resolutions. Extrapolating from the size, of the anomalous signal for copper (f" approximately 4 e-), this result, suggests that the approach could be used for proteins with molecular, weights of up to 33 kDa per Se (f"max++ = 8 e- at the 'white line') and 80, kDa for a Pt derivative (f"max = 19 e- at the 'white line', L3 edge). The, method provides a powerful alternative in solving a de novo protein, structure without either preparing multiple crystals (i.e. isomorphous, heavy-atom derivative plus native crystals) or collecting multi-wavelength, anomalous diffraction (MAD) data.
About this Structure
1A8Z is a Single protein structure of sequence from Acidithiobacillus ferrooxidans with CU1 as ligand. Full crystallographic information is available from OCA.
Reference
Structure determination of a 16.8 kDa copper protein at 2.1 A resolution using anomalous scattering data with direct methods., Harvey I, Hao Q, Duke EM, Ingledew WJ, Hasnain SS, Acta Crystallogr D Biol Crystallogr. 1998 Jul 1;54(Pt 4):629-35. PMID:9761859
Page seeded by OCA on Tue Nov 20 10:41:20 2007
