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Isolation, crystallization and preliminary X-ray diffraction analysis of L-amino-acid oxidase from Vipera ammodytes ammodytes venom.

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Isolation, crystallization and preliminary X-ray diffraction analysis of L-amino-acid oxidase from Vipera ammodytes ammodytes venom. / Georgieva, Dessislava; Kardas, Anna; Buck, Friedrich; Perbandt, Markus; Betzel, Christian.

In: ACTA CRYSTALLOGR F, Vol. 64, No. 10, 10, 2008, p. 918-921.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Georgieva, D, Kardas, A, Buck, F, Perbandt, M & Betzel, C 2008, 'Isolation, crystallization and preliminary X-ray diffraction analysis of L-amino-acid oxidase from Vipera ammodytes ammodytes venom.', ACTA CRYSTALLOGR F, vol. 64, no. 10, 10, pp. 918-921. <http://www.ncbi.nlm.nih.gov/pubmed/18931435?dopt=Citation>

APA

Georgieva, D., Kardas, A., Buck, F., Perbandt, M., & Betzel, C. (2008). Isolation, crystallization and preliminary X-ray diffraction analysis of L-amino-acid oxidase from Vipera ammodytes ammodytes venom. ACTA CRYSTALLOGR F, 64(10), 918-921. [10]. http://www.ncbi.nlm.nih.gov/pubmed/18931435?dopt=Citation

Vancouver

Georgieva D, Kardas A, Buck F, Perbandt M, Betzel C. Isolation, crystallization and preliminary X-ray diffraction analysis of L-amino-acid oxidase from Vipera ammodytes ammodytes venom. ACTA CRYSTALLOGR F. 2008;64(10):918-921. 10.

Bibtex

@article{6bcecc7bda32445d8c1136ac6a653182,
title = "Isolation, crystallization and preliminary X-ray diffraction analysis of L-amino-acid oxidase from Vipera ammodytes ammodytes venom.",
abstract = "L-Amino-acid oxidase from the venom of Vipera ammodytes ammodytes, the most venomous snake in Europe, was isolated and crystallized using the sitting-drop vapour-diffusion method. The solution conditions under which the protein sample was monodisperse were optimized using dynamic light scattering prior to crystallization. The crystals belonged to space group C2, with unit-cell parameters a = 198.37, b = 96.38, c = 109.11 A, beta = 92.56 degrees . Initial diffraction data were collected to 2.6 A resolution. The calculated Matthews coefficient is approximately 2.6 A(3) Da(-1) assuming the presence of four molecules in the asymmetric unit.",
author = "Dessislava Georgieva and Anna Kardas and Friedrich Buck and Markus Perbandt and Christian Betzel",
year = "2008",
language = "Deutsch",
volume = "64",
pages = "918--921",
journal = "ACTA CRYSTALLOGR F",
issn = "2053-230X",
publisher = "John Wiley and Sons Ltd",
number = "10",

}

RIS

TY - JOUR

T1 - Isolation, crystallization and preliminary X-ray diffraction analysis of L-amino-acid oxidase from Vipera ammodytes ammodytes venom.

AU - Georgieva, Dessislava

AU - Kardas, Anna

AU - Buck, Friedrich

AU - Perbandt, Markus

AU - Betzel, Christian

PY - 2008

Y1 - 2008

N2 - L-Amino-acid oxidase from the venom of Vipera ammodytes ammodytes, the most venomous snake in Europe, was isolated and crystallized using the sitting-drop vapour-diffusion method. The solution conditions under which the protein sample was monodisperse were optimized using dynamic light scattering prior to crystallization. The crystals belonged to space group C2, with unit-cell parameters a = 198.37, b = 96.38, c = 109.11 A, beta = 92.56 degrees . Initial diffraction data were collected to 2.6 A resolution. The calculated Matthews coefficient is approximately 2.6 A(3) Da(-1) assuming the presence of four molecules in the asymmetric unit.

AB - L-Amino-acid oxidase from the venom of Vipera ammodytes ammodytes, the most venomous snake in Europe, was isolated and crystallized using the sitting-drop vapour-diffusion method. The solution conditions under which the protein sample was monodisperse were optimized using dynamic light scattering prior to crystallization. The crystals belonged to space group C2, with unit-cell parameters a = 198.37, b = 96.38, c = 109.11 A, beta = 92.56 degrees . Initial diffraction data were collected to 2.6 A resolution. The calculated Matthews coefficient is approximately 2.6 A(3) Da(-1) assuming the presence of four molecules in the asymmetric unit.

M3 - SCORING: Zeitschriftenaufsatz

VL - 64

SP - 918

EP - 921

JO - ACTA CRYSTALLOGR F

JF - ACTA CRYSTALLOGR F

SN - 2053-230X

IS - 10

M1 - 10

ER -