DIRECT PHASING OF
ONE-WAVELENGTH ANOMALOUS SCATTERING DATA
Quan Hao1, Ian Harvey1,2, Elizabeth M. H. Duke2, W. John Ingledew3 and S. Samar Hasnain1,2
1Faculty of Applied Sciences, De Montfort
University, The Gateway, Leicester, LE1 9BH, U.K.
2CLRC Daresbury Laboratory, Warrington, WA4 4AD, U.K.
3School of Biomedical Sciences, St. Andrews
University, St. Andrews, Fife, KY16 9TS U.K.
The structure of rusticyanin, an acid stable copper protein,
has been determined at 2.1Å resolution by direct methods using
the single wavelength anomalous scattering (SAS) of copper (f''
=3.9e-). This is the largest unknown protein
structure (MW ~16.8kDa) to be determined using the direct methods
approach and it has been demonstrated that by exploiting the
anomalous signal at a single wavelength, direct methods can be
used to determine phases at typical (~2Å) macromolecular
crystallographic resolutions.