Crystallization of quinohaemoprotein alcohol dehydrogenase from Comamonas testosteroni: Crystals with unique optical properties

A. Oubrie; E.G. Huizinga; H.J. Rozeboom; K.H. Kalk; G.A.H. De Jong; J.A. Duine; B.W. Dijkstra

doi:10.1107/S0907444901013002

Crystallization of quinohaemoprotein alcohol dehydrogenase from Comamonas testosteroni: Crystals with unique optical properties

A. Oubrie
, E.G. Huizinga
, H.J. Rozeboom
, K.H. Kalk
, G.A.H. De Jong
, J.A. Duine
, B.W. Dijkstra

extern
University of Groningen

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

Abstract

Quinohaemoprotein alcohol dehydrogenase from Comamonas testosteroni is a functional electron-transfer protein containing both a haem c and a pyrroloquinoline quinone cofactor. The enzyme has been crystallized at 277 K using polyethylene glycol 6000 as precipitant. The crystals belong to space group C2, with unit-cell parameters a = 98.1, b = 74.3, c = 92.2 Å, β = 105.9°. A native data set with a resolution of 2.44 Å resolution has been collected. The approximate orientation of the haem group with respect to the unit-cell axes has been determined from the optical properties of the crystals.

Original language	English
Pages (from-to)	1732-1734
Number of pages	3
Journal	Acta crystallographica. Section D, biological crystallography
Volume	57
Issue number	11
DOIs	https://doi.org/10.1107/S0907444901013002
Publication status	Published - 22 Dec 2001
Externally published	Yes

Keywords

alcohol dehydrogenase
alcohol dehydrogenase (acceptor)
article
chemistry
Comamonas testosteroni
crystallization
enzymology
protein conformation
X ray crystallography

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10.1107/S0907444901013002

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Oubrie, A., Huizinga, E. G., Rozeboom, H. J., Kalk, K. H., De Jong, G. A. H., Duine, J. A., & Dijkstra, B. W. (2001). Crystallization of quinohaemoprotein alcohol dehydrogenase from Comamonas testosteroni: Crystals with unique optical properties. Acta crystallographica. Section D, biological crystallography, 57(11), 1732-1734. https://doi.org/10.1107/S0907444901013002

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title = "Crystallization of quinohaemoprotein alcohol dehydrogenase from Comamonas testosteroni: Crystals with unique optical properties",

abstract = "Quinohaemoprotein alcohol dehydrogenase from Comamonas testosteroni is a functional electron-transfer protein containing both a haem c and a pyrroloquinoline quinone cofactor. The enzyme has been crystallized at 277 K using polyethylene glycol 6000 as precipitant. The crystals belong to space group C2, with unit-cell parameters a = 98.1, b = 74.3, c = 92.2 {\AA}, β = 105.9°. A native data set with a resolution of 2.44 {\AA} resolution has been collected. The approximate orientation of the haem group with respect to the unit-cell axes has been determined from the optical properties of the crystals.",

keywords = "alcohol dehydrogenase, alcohol dehydrogenase (acceptor), article, chemistry, Comamonas testosteroni, crystallization, enzymology, protein conformation, X ray crystallography",

author = "A. Oubrie and E.G. Huizinga and H.J. Rozeboom and K.H. Kalk and \{De Jong\}, G.A.H. and J.A. Duine and B.W. Dijkstra",

year = "2001",

month = dec,

day = "22",

doi = "10.1107/S0907444901013002",

language = "English",

volume = "57",

pages = "1732--1734",

journal = "Acta crystallographica. Section D, biological crystallography",

issn = "0907-4449",

publisher = "International Union of Crystallography",

number = "11",

}

Crystallization of quinohaemoprotein alcohol dehydrogenase from Comamonas testosteroni: Crystals with unique optical properties. / Oubrie, A.; Huizinga, E.G.; Rozeboom, H.J. et al.
In: Acta crystallographica. Section D, biological crystallography, Vol. 57, No. 11, 22.12.2001, p. 1732-1734.

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

TY - JOUR

T1 - Crystallization of quinohaemoprotein alcohol dehydrogenase from Comamonas testosteroni: Crystals with unique optical properties

AU - Oubrie, A.

AU - Huizinga, E.G.

AU - Rozeboom, H.J.

AU - Kalk, K.H.

AU - De Jong, G.A.H.

AU - Duine, J.A.

AU - Dijkstra, B.W.

PY - 2001/12/22

Y1 - 2001/12/22

N2 - Quinohaemoprotein alcohol dehydrogenase from Comamonas testosteroni is a functional electron-transfer protein containing both a haem c and a pyrroloquinoline quinone cofactor. The enzyme has been crystallized at 277 K using polyethylene glycol 6000 as precipitant. The crystals belong to space group C2, with unit-cell parameters a = 98.1, b = 74.3, c = 92.2 Å, β = 105.9°. A native data set with a resolution of 2.44 Å resolution has been collected. The approximate orientation of the haem group with respect to the unit-cell axes has been determined from the optical properties of the crystals.

AB - Quinohaemoprotein alcohol dehydrogenase from Comamonas testosteroni is a functional electron-transfer protein containing both a haem c and a pyrroloquinoline quinone cofactor. The enzyme has been crystallized at 277 K using polyethylene glycol 6000 as precipitant. The crystals belong to space group C2, with unit-cell parameters a = 98.1, b = 74.3, c = 92.2 Å, β = 105.9°. A native data set with a resolution of 2.44 Å resolution has been collected. The approximate orientation of the haem group with respect to the unit-cell axes has been determined from the optical properties of the crystals.

KW - alcohol dehydrogenase

KW - alcohol dehydrogenase (acceptor)

KW - article

KW - chemistry

KW - Comamonas testosteroni

KW - crystallization

KW - enzymology

KW - protein conformation

KW - X ray crystallography

U2 - 10.1107/S0907444901013002

DO - 10.1107/S0907444901013002

M3 - Article

SN - 0907-4449

VL - 57

SP - 1732

EP - 1734

JO - Acta crystallographica. Section D, biological crystallography

JF - Acta crystallographica. Section D, biological crystallography

IS - 11

ER -

Crystallization of quinohaemoprotein alcohol dehydrogenase from Comamonas testosteroni: Crystals with unique optical properties

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Keywords

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