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May 25, 2012
In the May 25 issue of Science (Liu, et al, Science, 336, 1033-1037, 2012), the Hendrickson group describes novel synchrotron experiments that permit routine structure determinations for generic native macromolecules without the need to incorporate heavy atoms. Sulfur and other light atoms are first located based on their anomalous scattering, and then the entire atomic structure follows. Above is a detail from an artistic rendering by Irving Geis, showing the atomic structure of crambin ‘illuminated’ by the sulfur atoms used to determine its structure. The crystal structure of crambin (Hendrickson & Teeter, Nature, 290, 107, 1981) was the first to be solved by what is now known as single-wavelength anomalous diffraction (SAD). Crambin is a small protein at exceptionally high resolution; broad adoption of native SAD for more typical problems has been hampered by weak signals and high diffraction noise. The new methods address these complications.
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