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Phasing on anomalous signal of sulfurs: What is the limit?



Phasing on anomalous signal of sulfurs: What is the limit?



Acta Crystallographica Section D Biological Crystallography 59(6): 1020-1027



Recent years have witnessed significant advancements in X-ray data-acquisition techniques and phasing algorithms, which have made possible the successful use of a very small anomalous diffraction signal for the solution of crystal structures of macromolecules. Two crystal structures, a 44 kDa glucose isomerase containing nine sulfurs and a 33 kDa xylanase containing five sulfurs, have been solved from single-wavelength anomalous data using widely available methods and programs. These two enzymes contain less sulfur than most proteins in the bacterial or eukaryotic proteomes, providing a Bijvoet ratio of about 0.6%. For glucose isomerase the automatically interpretable electron-density maps could be obtained at high as well as low resolution. The S-SAD approach relies on the anomalous signal of sulfur naturally occurring in proteins and alleviates all need for sample derivatization. It may therefore be applicable to all protein crystals able to provide accurate diffraction data.

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Accession: 011140696

Download citation: RISBibTeXText

PMID: 12777765

DOI: 10.1107/s0907444903007467


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