Crystallization and preliminary crystallographic analysis of an NADH oxidase that functions in peroxide reduction in Thermus aquaticus YT-1

Aengus MacSweeney; Allan D'Arcy; Timothy M. Higgins; Stephen G. Mayhew; David Toomey; Martin A. Walsh

doi:10.13025/24008

Crystallization and preliminary crystallographic analysis of an NADH oxidase that functions in peroxide reduction in Thermus aquaticus YT-1

Aengus MacSweeney
, Allan D'Arcy
, Timothy M. Higgins
, Stephen G. Mayhew
, David Toomey
, Martin A. Walsh

Cellular & Molecular Medicine

Research output: Contribution to a Journal (Peer & Non Peer) › Article › peer-review

1 Citation (Scopus)

Abstract

NADH oxidase from Thermus aquaticus is a thermostable flavoenzyme that is similar in amino-acid sequence and other properties to the flavoenzyme component of the NADH peroxidase systems from Salmonella typhimurium and Amphibacillus xylanus. The enzyme has been isolated from T. aquaticus and crystallized using the hanging-drop method of vapour diffusion with sodium citrate as a precipitant at pH 8.5. The crystals belong to the hexagonal space group P622 with unit-cell dimensions a = b = 89.9, c = 491.6 Angstrom, and diffract to 2.5 Angstrom resolution.

Original language	English (Ireland)
Number of pages	2
Journal	ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
Volume	55
DOIs	https://doi.org/10.13025/24008 https://doi.org/10.1107/s090744499800941x
Publication status	Published - 1 Jan 1999

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10.13025/24008Licence: CC BY-NC-ND
10.1107/s090744499800941x

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MacSweeney, A., D'Arcy, A., Higgins, T. M., Mayhew, S. G., Toomey, D., & Walsh, M. A. (1999). Crystallization and preliminary crystallographic analysis of an NADH oxidase that functions in peroxide reduction in Thermus aquaticus YT-1. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 55. https://doi.org/10.13025/24008, https://doi.org/10.1107/s090744499800941x

@article{a65fe62dd9754b0096fffbbf997ef1d0,

title = "Crystallization and preliminary crystallographic analysis of an NADH oxidase that functions in peroxide reduction in Thermus aquaticus YT-1",

abstract = "NADH oxidase from Thermus aquaticus is a thermostable flavoenzyme that is similar in amino-acid sequence and other properties to the flavoenzyme component of the NADH peroxidase systems from Salmonella typhimurium and Amphibacillus xylanus. The enzyme has been isolated from T. aquaticus and crystallized using the hanging-drop method of vapour diffusion with sodium citrate as a precipitant at pH 8.5. The crystals belong to the hexagonal space group P622 with unit-cell dimensions a = b = 89.9, c = 491.6 Angstrom, and diffract to 2.5 Angstrom resolution.",

author = "Aengus MacSweeney and Allan D'Arcy and Higgins, \{Timothy M.\} and Mayhew, \{Stephen G.\} and David Toomey and Walsh, \{Martin A.\}",

year = "1999",

month = jan,

day = "1",

doi = "10.13025/24008",

language = "English (Ireland)",

volume = "55",

journal = "ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY",

}

Crystallization and preliminary crystallographic analysis of an NADH oxidase that functions in peroxide reduction in Thermus aquaticus YT-1. / MacSweeney, Aengus; D'Arcy, Allan; Higgins, Timothy M. et al.
In: ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, Vol. 55, 01.01.1999.

Research output: Contribution to a Journal (Peer & Non Peer) › Article › peer-review

TY - JOUR

T1 - Crystallization and preliminary crystallographic analysis of an NADH oxidase that functions in peroxide reduction in Thermus aquaticus YT-1

AU - MacSweeney, Aengus

AU - D'Arcy, Allan

AU - Higgins, Timothy M.

AU - Mayhew, Stephen G.

AU - Toomey, David

AU - Walsh, Martin A.

PY - 1999/1/1

Y1 - 1999/1/1

N2 - NADH oxidase from Thermus aquaticus is a thermostable flavoenzyme that is similar in amino-acid sequence and other properties to the flavoenzyme component of the NADH peroxidase systems from Salmonella typhimurium and Amphibacillus xylanus. The enzyme has been isolated from T. aquaticus and crystallized using the hanging-drop method of vapour diffusion with sodium citrate as a precipitant at pH 8.5. The crystals belong to the hexagonal space group P622 with unit-cell dimensions a = b = 89.9, c = 491.6 Angstrom, and diffract to 2.5 Angstrom resolution.

AB - NADH oxidase from Thermus aquaticus is a thermostable flavoenzyme that is similar in amino-acid sequence and other properties to the flavoenzyme component of the NADH peroxidase systems from Salmonella typhimurium and Amphibacillus xylanus. The enzyme has been isolated from T. aquaticus and crystallized using the hanging-drop method of vapour diffusion with sodium citrate as a precipitant at pH 8.5. The crystals belong to the hexagonal space group P622 with unit-cell dimensions a = b = 89.9, c = 491.6 Angstrom, and diffract to 2.5 Angstrom resolution.

UR - http://hdl.handle.net/10379/9462

U2 - 10.13025/24008

DO - 10.13025/24008

M3 - Article

VL - 55

JO - ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

JF - ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

ER -

Crystallization and preliminary crystallographic analysis of an NADH oxidase that functions in peroxide reduction in Thermus aquaticus YT-1

Abstract

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