In-house zinc sad phasing at Cu K? Edge

Min Kyu Kim; Sangmin Lee; Young Jun An; Chang Sook Jeong; Chang Jun Ji; Jin Won Lee; Sun Shin Cha

doi:10.1007/s10059-013-0074-1

In-house zinc sad phasing at Cu K? Edge

Min Kyu Kim, Sangmin Lee, Young Jun An, Chang Sook Jeong, Chang Jun Ji, Jin Won Lee, Sun Shin Cha

Department of Chemistry & Nanoscience

Research output: Contribution to journal › Article › peer-review

6 Scopus citations

Abstract

De novo zinc single-wavelength anomalous dispersion (Zn-SAD) phasing has been demonstrated with the 1.9 A resolution data of glucose isomerase and 2.6 A resolution data of Staphylococcus aureus Fur (SaFur) collected using in-house Cu K? 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 A resolution SAD data indicate that inhouse Zn-SAD phasing can be widely applicable to structure determination.

Original language	English
Pages (from-to)	74-81
Number of pages	8
Journal	Molecules and Cells
Volume	36
Issue number	1
DOIs	https://doi.org/10.1007/s10059-013-0074-1
State	Published - Jul 2013

Bibliographical note

Funding Information:
This work was supported by the National Research Foundation of Korea Grant 2012005978, the CAP through Korea Research Council of Fundamental Science Technology (KRCF), Korea Institute of Science and Technology (KIST), & Korea Institute of Ocean Science and Technology (KIOST), the Marine and Extreme Genome Research Center program and the Development of Biohydrogen Production Technology Using Hyperthermophilic Archaea program of MLTM, and the KIOST in-house NSC program. The work performed at Hanyang University was supported by the Korea Research Foundation Grant funded by the Korean Goverment (KRF-2008-313-C00774) and by Mid-career Researcher Program through NRF grant funded by the [The Ministry of Education, Science and Technology (MEST)] (NRF-2012-0005445).

Keywords

Anomalous Scattering
Experimental Phasing
Protein Crystallography
Sad Phasing
Zinc

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title = "In-house zinc sad phasing at Cu K? Edge",

abstract = "De novo zinc single-wavelength anomalous dispersion (Zn-SAD) phasing has been demonstrated with the 1.9 A resolution data of glucose isomerase and 2.6 A resolution data of Staphylococcus aureus Fur (SaFur) collected using in-house Cu K? 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 A 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",

author = "Kim, {Min Kyu} and Sangmin Lee and An, {Young Jun} and Jeong, {Chang Sook} and Ji, {Chang Jun} and Lee, {Jin Won} and Cha, {Sun Shin}",

note = "Funding Information: This work was supported by the National Research Foundation of Korea Grant 2012005978, the CAP through Korea Research Council of Fundamental Science Technology (KRCF), Korea Institute of Science and Technology (KIST), & Korea Institute of Ocean Science and Technology (KIOST), the Marine and Extreme Genome Research Center program and the Development of Biohydrogen Production Technology Using Hyperthermophilic Archaea program of MLTM, and the KIOST in-house NSC program. The work performed at Hanyang University was supported by the Korea Research Foundation Grant funded by the Korean Goverment (KRF-2008-313-C00774) and by Mid-career Researcher Program through NRF grant funded by the [The Ministry of Education, Science and Technology (MEST)] (NRF-2012-0005445).",

year = "2013",

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doi = "10.1007/s10059-013-0074-1",

language = "English",

volume = "36",

pages = "74--81",

journal = "Molecules and Cells",

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AU - Kim, Min Kyu

AU - Lee, Sangmin

AU - An, Young Jun

AU - Jeong, Chang Sook

AU - Ji, Chang Jun

AU - Lee, Jin Won

AU - Cha, Sun Shin

N1 - Funding Information: This work was supported by the National Research Foundation of Korea Grant 2012005978, the CAP through Korea Research Council of Fundamental Science Technology (KRCF), Korea Institute of Science and Technology (KIST), & Korea Institute of Ocean Science and Technology (KIOST), the Marine and Extreme Genome Research Center program and the Development of Biohydrogen Production Technology Using Hyperthermophilic Archaea program of MLTM, and the KIOST in-house NSC program. The work performed at Hanyang University was supported by the Korea Research Foundation Grant funded by the Korean Goverment (KRF-2008-313-C00774) and by Mid-career Researcher Program through NRF grant funded by the [The Ministry of Education, Science and Technology (MEST)] (NRF-2012-0005445).

PY - 2013/7

Y1 - 2013/7

N2 - De novo zinc single-wavelength anomalous dispersion (Zn-SAD) phasing has been demonstrated with the 1.9 A resolution data of glucose isomerase and 2.6 A resolution data of Staphylococcus aureus Fur (SaFur) collected using in-house Cu K? 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 A resolution SAD data indicate that inhouse Zn-SAD phasing can be widely applicable to structure determination.

AB - De novo zinc single-wavelength anomalous dispersion (Zn-SAD) phasing has been demonstrated with the 1.9 A resolution data of glucose isomerase and 2.6 A resolution data of Staphylococcus aureus Fur (SaFur) collected using in-house Cu K? 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 A resolution SAD data indicate that inhouse Zn-SAD phasing can be widely applicable to structure determination.

KW - Anomalous Scattering

KW - Experimental Phasing

KW - Protein Crystallography

KW - Sad Phasing

KW - Zinc

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SP - 74

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JO - Molecules and Cells

JF - Molecules and Cells

IS - 1

ER -

In-house zinc sad phasing at Cu K? Edge

Abstract

Bibliographical note

Keywords

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