Crystallization and preliminary X-ray crystallographic analysis of human nucleoside diphosphate kinase A

Kyeongsik Min; Sun Young Kim; Hyun Kyu Song; Changsoo Chang; Seung Je Cho; Jinho Moon; Jin Kuk Yang; Jae Young Lee; Kong Joo Lee; Se Won Suh

doi:10.1107/S0907444900002626

Crystallization and preliminary X-ray crystallographic analysis of human nucleoside diphosphate kinase A

Kyeongsik Min, Sun Young Kim, Hyun Kyu Song, Changsoo Chang, Seung Je Cho, Jinho Moon, Jin Kuk Yang, Jae Young Lee, Kong Joo Lee, Se Won Suh

Department of Life Science

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

6 Scopus citations

Abstract

Human nucleoside diphosphate kinase A catalyzes phosphoryl transfer and acts as a suppressor of metastasis. It has been crystallized using 2-methyl-2,4-pentanediol as a precipitant at 288 K. The crystal is monoclinic, belonging to the space group P2₁, with unit-cell parameters a = 74.21, b = 78.11, c = 82.29 Å, β = 101.33°. The asymmetric unit contains a homohexamer, with a corresponding crystal volume per protein mass (V(m)) of 2.27 Å³ Da^-1 and a solvent content of 46%. Native X-ray data to 2.15 Å resolution have been collected using synchrotron X-rays.

Original language	English
Pages (from-to)	504-505
Number of pages	2
Journal	Acta Crystallographica Section D: Biological Crystallography
Volume	56
Issue number	4
DOIs	https://doi.org/10.1107/S0907444900002626
State	Published - 2000

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title = "Crystallization and preliminary X-ray crystallographic analysis of human nucleoside diphosphate kinase A",

abstract = "Human nucleoside diphosphate kinase A catalyzes phosphoryl transfer and acts as a suppressor of metastasis. It has been crystallized using 2-methyl-2,4-pentanediol as a precipitant at 288 K. The crystal is monoclinic, belonging to the space group P21, with unit-cell parameters a = 74.21, b = 78.11, c = 82.29 {\AA}, β = 101.33°. The asymmetric unit contains a homohexamer, with a corresponding crystal volume per protein mass (V(m)) of 2.27 {\AA}3 Da-1 and a solvent content of 46%. Native X-ray data to 2.15 {\AA} resolution have been collected using synchrotron X-rays.",

author = "Kyeongsik Min and Kim, {Sun Young} and Song, {Hyun Kyu} and Changsoo Chang and Cho, {Seung Je} and Jinho Moon and Yang, {Jin Kuk} and Lee, {Jae Young} and Lee, {Kong Joo} and Suh, {Se Won}",

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T1 - Crystallization and preliminary X-ray crystallographic analysis of human nucleoside diphosphate kinase A

AU - Min, Kyeongsik

AU - Kim, Sun Young

AU - Song, Hyun Kyu

AU - Chang, Changsoo

AU - Cho, Seung Je

AU - Moon, Jinho

AU - Yang, Jin Kuk

AU - Lee, Jae Young

AU - Lee, Kong Joo

AU - Suh, Se Won

PY - 2000

Y1 - 2000

N2 - Human nucleoside diphosphate kinase A catalyzes phosphoryl transfer and acts as a suppressor of metastasis. It has been crystallized using 2-methyl-2,4-pentanediol as a precipitant at 288 K. The crystal is monoclinic, belonging to the space group P21, with unit-cell parameters a = 74.21, b = 78.11, c = 82.29 Å, β = 101.33°. The asymmetric unit contains a homohexamer, with a corresponding crystal volume per protein mass (V(m)) of 2.27 Å3 Da-1 and a solvent content of 46%. Native X-ray data to 2.15 Å resolution have been collected using synchrotron X-rays.

AB - Human nucleoside diphosphate kinase A catalyzes phosphoryl transfer and acts as a suppressor of metastasis. It has been crystallized using 2-methyl-2,4-pentanediol as a precipitant at 288 K. The crystal is monoclinic, belonging to the space group P21, with unit-cell parameters a = 74.21, b = 78.11, c = 82.29 Å, β = 101.33°. The asymmetric unit contains a homohexamer, with a corresponding crystal volume per protein mass (V(m)) of 2.27 Å3 Da-1 and a solvent content of 46%. Native X-ray data to 2.15 Å resolution have been collected using synchrotron X-rays.

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DO - 10.1107/S0907444900002626

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JO - Acta Crystallographica Section D: Biological Crystallography

JF - Acta Crystallographica Section D: Biological Crystallography

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ER -

Crystallization and preliminary X-ray crystallographic analysis of human nucleoside diphosphate kinase A

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