Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of human dihydrouridine synthase

Sam Griffiths; Robert T Byrne; Alfred A Antson; Fiona Whelan

doi:10.1107/S1744309112003831

Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of human dihydrouridine synthase

Sam Griffiths, Robert T Byrne, Alfred A Antson, Fiona Whelan

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

Abstract

Dihydrouridine synthases catalyse the reduction of uridine to dihydrouridine in the D-loop and variable loop of tRNA. The human dihydrouridine synthase HsDus2L has been implicated in the development of pulmonary carcinogenesis. Here, the purification, crystallization and preliminary X-ray characterization of the HsDus2L catalytic domain are reported. The crystals belonged to space group P2(1) and contained a single molecule of HsDus2L in the asymmetric unit. A complete data set was collected to 1.9 Å resolution using synchrotron radiation.

Original language	English
Pages (from-to)	333-336
Number of pages	4
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	68
Issue number	Pt 3
Early online date	22 Feb 2012
DOIs	https://doi.org/10.1107/S1744309112003831
Publication status	Published - 2012

Bibliographical note

Keywords

Catalytic Domain
Crystallization
Crystallography, X-Ray
Humans
Oxidoreductases

Access to Document

10.1107/S1744309112003831

Cite this

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title = "Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of human dihydrouridine synthase",

abstract = "Dihydrouridine synthases catalyse the reduction of uridine to dihydrouridine in the D-loop and variable loop of tRNA. The human dihydrouridine synthase HsDus2L has been implicated in the development of pulmonary carcinogenesis. Here, the purification, crystallization and preliminary X-ray characterization of the HsDus2L catalytic domain are reported. The crystals belonged to space group P2(1) and contained a single molecule of HsDus2L in the asymmetric unit. A complete data set was collected to 1.9 {\AA} resolution using synchrotron radiation.",

keywords = "Catalytic Domain, Crystallization, Crystallography, X-Ray, Humans, Oxidoreductases",

author = "Sam Griffiths and Byrne, {Robert T} and Antson, {Alfred A} and Fiona Whelan",

note = "{\textcopyright} 2012 International Union of Crystallography",

year = "2012",

doi = "10.1107/S1744309112003831",

language = "English",

volume = "68",

pages = "333--336",

journal = "Acta Crystallographica Section F: Structural Biology and Crystallization Communications",

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publisher = "Wiley-Blackwell",

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Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of human dihydrouridine synthase. / Griffiths, Sam; Byrne, Robert T; Antson, Alfred A et al.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 68, No. Pt 3, 2012, p. 333-336.

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

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T1 - Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of human dihydrouridine synthase

AU - Griffiths, Sam

AU - Byrne, Robert T

AU - Antson, Alfred A

AU - Whelan, Fiona

PY - 2012

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AB - Dihydrouridine synthases catalyse the reduction of uridine to dihydrouridine in the D-loop and variable loop of tRNA. The human dihydrouridine synthase HsDus2L has been implicated in the development of pulmonary carcinogenesis. Here, the purification, crystallization and preliminary X-ray characterization of the HsDus2L catalytic domain are reported. The crystals belonged to space group P2(1) and contained a single molecule of HsDus2L in the asymmetric unit. A complete data set was collected to 1.9 Å resolution using synchrotron radiation.

KW - Catalytic Domain

KW - Crystallization

KW - Crystallography, X-Ray

KW - Humans

KW - Oxidoreductases

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JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

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