Crystallization and preliminary X-ray crystallographic analysis of NAD+-dependent DNA ligase from Thermus filiformis

Jae Young Lee; Hyun Kyu Kim; Changsoo Chang; Soo Hyun Eom; Kwang Yeon Hwang; Yunje Cho; Yeon Gyu Yu; Seong Eon Ryu; Suk Tae Kwon; Se Won Suh

doi:10.1107/S090744490000010X

Crystallization and preliminary X-ray crystallographic analysis of NAD⁺-dependent DNA ligase from Thermus filiformis

Jae Young Lee, Hyun Kyu Kim, Changsoo Chang, Soo Hyun Eom, Kwang Yeon Hwang, Yunje Cho, Yeon Gyu Yu, Seong Eon Ryu, Suk Tae Kwon, Se Won Suh

Department of Biosystems and Biotechnology

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

2 Citations (Scopus)

Abstract

A highly thermostable DNA ligase from Thermus filiformis has been crystallized at room temperature using methoxypolyethylene glycol 5000 as a precipitant. The crystal belongs to the monoclinic space group P2₁, with unit-cell parameters a = 90.63, b = 117.80, c = 98.65 Å, β = 115.56°. Two molecules of DNA ligase are present in the asymmetric unit, giving a crystal volume per protein mass (V(m)) of 3.1 Å₃Da^-1 and a solvent content of 61%. A native data set extending to 3.0 Å resolution has been collected at 100 K using synchrotron X-rays.

Original language	English
Pages (from-to)	357-358
Number of pages	2
Journal	Acta Crystallographica Section D: Biological Crystallography
Volume	56
Issue number	3
DOIs	https://doi.org/10.1107/S090744490000010X
Publication status	Published - 2000

ASJC Scopus subject areas

Structural Biology

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10.1107/S090744490000010X

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title = "Crystallization and preliminary X-ray crystallographic analysis of NAD+-dependent DNA ligase from Thermus filiformis",

abstract = "A highly thermostable DNA ligase from Thermus filiformis has been crystallized at room temperature using methoxypolyethylene glycol 5000 as a precipitant. The crystal belongs to the monoclinic space group P21, with unit-cell parameters a = 90.63, b = 117.80, c = 98.65 {\AA}, β = 115.56°. Two molecules of DNA ligase are present in the asymmetric unit, giving a crystal volume per protein mass (V(m)) of 3.1 {\AA}3Da-1 and a solvent content of 61%. A native data set extending to 3.0 {\AA} resolution has been collected at 100 K using synchrotron X-rays.",

author = "Lee, {Jae Young} and Kim, {Hyun Kyu} and Changsoo Chang and Eom, {Soo Hyun} and Hwang, {Kwang Yeon} and Yunje Cho and Yu, {Yeon Gyu} and Ryu, {Seong Eon} and Kwon, {Suk Tae} and Suh, {Se Won}",

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doi = "10.1107/S090744490000010X",

language = "English",

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journal = "Acta Crystallographica Section D: Structural Biology",

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T1 - Crystallization and preliminary X-ray crystallographic analysis of NAD+-dependent DNA ligase from Thermus filiformis

AU - Lee, Jae Young

AU - Kim, Hyun Kyu

AU - Chang, Changsoo

AU - Eom, Soo Hyun

AU - Hwang, Kwang Yeon

AU - Cho, Yunje

AU - Yu, Yeon Gyu

AU - Ryu, Seong Eon

AU - Kwon, Suk Tae

AU - Suh, Se Won

PY - 2000

Y1 - 2000

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AB - A highly thermostable DNA ligase from Thermus filiformis has been crystallized at room temperature using methoxypolyethylene glycol 5000 as a precipitant. The crystal belongs to the monoclinic space group P21, with unit-cell parameters a = 90.63, b = 117.80, c = 98.65 Å, β = 115.56°. Two molecules of DNA ligase are present in the asymmetric unit, giving a crystal volume per protein mass (V(m)) of 3.1 Å3Da-1 and a solvent content of 61%. A native data set extending to 3.0 Å resolution has been collected at 100 K using synchrotron X-rays.

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JO - Acta Crystallographica Section D: Structural Biology

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Crystallization and preliminary X-ray crystallographic analysis of NAD⁺-dependent DNA ligase from Thermus filiformis

Abstract

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