Mol. Cells 2013; 36(1): 74-81
Published online May 16, 2013
https://doi.org/10.1007/s10059-013-0074-1
© The Korean Society for Molecular and Cellular Biology
De novo zinc single-wavelength anomalous dispersion (Zn-SAD) phasing has been demonstrated with the 1.9 ? resolution data of glucose isomerase and 2.6 ? resolution data of Staphylococcus aureus Fur (SaFur) collected using in-house Cu Kα X-ray source. The successful in-house Zn- SAD phasing of glucose isomerase, based on the anomalous signals of both zinc ions introduced to crystals by soaking and native sulfur atoms, drove us to determine the structure of SaFur, a zinc-containing transcription factor, by Zn-SAD phasing using in-house X-ray source. The abundance of zinc-containing proteins in nature, the easy zinc derivatization of the protein surface, no need of synchrotron access, and the successful experimental phasing with the modest 2.6 ? resolution SAD data indicate that inhouse Zn-SAD phasing can be widely applicable to structure determination.
Keywords anomalous scattering, experimental phasing, protein crystallography, SAD phasing, zinc
Mol. Cells 2013; 36(1): 74-81
Published online July 31, 2013 https://doi.org/10.1007/s10059-013-0074-1
Copyright © The Korean Society for Molecular and Cellular Biology.
Min-Kyu Kim, Sangmin Lee, Young Jun An, Chang-Sook Jeong, Chang-Jun Ji, Jin-Won Lee, and Sun-Shin Cha
1Marine Biotechnology Research Division, Korea Institute of Ocean Science and Technology, Ansan 426-744, Korea, 2Ocean Science and Technology School, Pusan 606-791, Korea, 3Department of Life Science and Institute for Natural Sciences, Hanyang University, Seoul 133-791, Korea, 4Department of Marine Biotechnology, University of Science and Technology, Daejeon 305-333 Korea, 5These authors contributed equally to this work.
De novo zinc single-wavelength anomalous dispersion (Zn-SAD) phasing has been demonstrated with the 1.9 ? resolution data of glucose isomerase and 2.6 ? resolution data of Staphylococcus aureus Fur (SaFur) collected using in-house Cu Kα X-ray source. The successful in-house Zn- SAD phasing of glucose isomerase, based on the anomalous signals of both zinc ions introduced to crystals by soaking and native sulfur atoms, drove us to determine the structure of SaFur, a zinc-containing transcription factor, by Zn-SAD phasing using in-house X-ray source. The abundance of zinc-containing proteins in nature, the easy zinc derivatization of the protein surface, no need of synchrotron access, and the successful experimental phasing with the modest 2.6 ? resolution SAD data indicate that inhouse Zn-SAD phasing can be widely applicable to structure determination.
Keywords: anomalous scattering, experimental phasing, protein crystallography, SAD phasing, zinc
Bonah Kim and Won-Woo Lee
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