1A8Z

STRUCTURE DETERMINATION OF A 16.8KDA COPPER PROTEIN RUSTICYANIN AT 2.1A RESOLUTION USING ANOMALOUS SCATTERING DATA WITH DIRECT METHODS

Summary for 1A8Z

• Entry DOI: 10.2210/pdb1a8z/pdb
• Descriptor: RUSTICYANIN, COPPER (I) ION (3 entities in total)
• Functional Keywords: direct methods, sas, medium resolution, metalloprotein, copper protein, electron transport
• Biological source: Acidithiobacillus ferrooxidans
• Cellular location: Periplasm: P24930
• Total number of polymer chains: 1
• Total formula weight: 16472.29

Authors

Harvey, I.,Hao, Q.,Duke, E.M.H.,Ingledew, W.J.,Hasnain, S.S. (deposition date: 1998-03-30, release date: 1998-06-17, Last modification date: 2024-02-07)

Primary citation

Harvey, I.,Hao, Q.,Duke, E.M.,Ingledew, W.J.,Hasnain, S.S.
Structure determination of a 16.8 kDa copper protein at 2.1 A resolution using anomalous scattering data with direct methods.
Acta Crystallogr.,Sect.D, 54:629-635, 1998

PubMed Abstract: 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.

PubMed: 9761859
DOI: 10.1107/S0907444998005423

Experimental method

X-RAY DIFFRACTION (2.1 Å)