Synchrotron radiation (SR) is an extremely useful X-ray source for protein crystallography. It is high brilliance, high intensity and small divergence white X-ray source, which enables us to collect high resolution diffraction data of biological macromolecular crystals with large cell dimensions. Furthermore, wavelength tunability of SR is essential for the phase determination by multiwavelength anomalous diffraction (MAD) method, which has a possibility of the direct phase determination of metal proteins, selenomethionyl proteins and proteins with single isomorphous derivative of poor isomorphism.
MAD method is applied for the structure determination of cytochrome
c-553 from
Desulfovibrio vulgaris Miyazaki F strain.
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