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Isolation, purification, crystallization and preliminary crystallographic studies of a chitinase from Crocus vernus.

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Isolation, purification, crystallization and preliminary crystallographic studies of a chitinase from Crocus vernus. / Akrem, Ahmed; Iqbal, Sadaf; Buck, Friedrich; Meyer, Arne; Perbandt, Markus; Voelter, Wolfgang; Betzel, Christian.

in: ACTA CRYSTALLOGR F, Jahrgang 67, Nr. Pt 3, Pt 3, 2011, S. 340-343.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Akrem, A, Iqbal, S, Buck, F, Meyer, A, Perbandt, M, Voelter, W & Betzel, C 2011, 'Isolation, purification, crystallization and preliminary crystallographic studies of a chitinase from Crocus vernus.', ACTA CRYSTALLOGR F, Jg. 67, Nr. Pt 3, Pt 3, S. 340-343. <http://www.ncbi.nlm.nih.gov/pubmed/21393839?dopt=Citation>

APA

Akrem, A., Iqbal, S., Buck, F., Meyer, A., Perbandt, M., Voelter, W., & Betzel, C. (2011). Isolation, purification, crystallization and preliminary crystallographic studies of a chitinase from Crocus vernus. ACTA CRYSTALLOGR F, 67(Pt 3), 340-343. [Pt 3]. http://www.ncbi.nlm.nih.gov/pubmed/21393839?dopt=Citation

Vancouver

Akrem A, Iqbal S, Buck F, Meyer A, Perbandt M, Voelter W et al. Isolation, purification, crystallization and preliminary crystallographic studies of a chitinase from Crocus vernus. ACTA CRYSTALLOGR F. 2011;67(Pt 3):340-343. Pt 3.

Bibtex

@article{8d71e92eedc44679ada9ade7aa1c7889,
title = "Isolation, purification, crystallization and preliminary crystallographic studies of a chitinase from Crocus vernus.",
abstract = "A chitinase has been isolated and purified from Crocus vernus corms. N-terminal amino-acid sequence analysis of the approximately 30?kDa protein showed 33% identity to narbonin, a seed protein from Vicia narbonensis L. The C. vernus chitinase was crystallized by the hanging-drop vapour-diffusion method using PEG 8000 as the main precipitant. The crystal belonged to the monoclinic space group C2, with unit-cell parameters a=172.3, b=37.1, c=126.4?{\AA}, ?=127° and two molecules per asymmetric unit. Diffraction data were collected to a resolution of 2.1?{\AA}.",
keywords = "Animals, Amino Acid Sequence, Molecular Sequence Data, Sequence Alignment, X-Ray Diffraction, Crystallography, X-Ray, Crystallization, Chitinase/*chemistry/genetics/*isolation & purification, Crocus/*enzymology, Globulins/genetics, Vegetable Proteins/genetics, Animals, Amino Acid Sequence, Molecular Sequence Data, Sequence Alignment, X-Ray Diffraction, Crystallography, X-Ray, Crystallization, Chitinase/*chemistry/genetics/*isolation & purification, Crocus/*enzymology, Globulins/genetics, Vegetable Proteins/genetics",
author = "Ahmed Akrem and Sadaf Iqbal and Friedrich Buck and Arne Meyer and Markus Perbandt and Wolfgang Voelter and Christian Betzel",
year = "2011",
language = "English",
volume = "67",
pages = "340--343",
journal = "ACTA CRYSTALLOGR F",
issn = "2053-230X",
publisher = "John Wiley and Sons Ltd",
number = "Pt 3",

}

RIS

TY - JOUR

T1 - Isolation, purification, crystallization and preliminary crystallographic studies of a chitinase from Crocus vernus.

AU - Akrem, Ahmed

AU - Iqbal, Sadaf

AU - Buck, Friedrich

AU - Meyer, Arne

AU - Perbandt, Markus

AU - Voelter, Wolfgang

AU - Betzel, Christian

PY - 2011

Y1 - 2011

N2 - A chitinase has been isolated and purified from Crocus vernus corms. N-terminal amino-acid sequence analysis of the approximately 30?kDa protein showed 33% identity to narbonin, a seed protein from Vicia narbonensis L. The C. vernus chitinase was crystallized by the hanging-drop vapour-diffusion method using PEG 8000 as the main precipitant. The crystal belonged to the monoclinic space group C2, with unit-cell parameters a=172.3, b=37.1, c=126.4?Å, ?=127° and two molecules per asymmetric unit. Diffraction data were collected to a resolution of 2.1?Å.

AB - A chitinase has been isolated and purified from Crocus vernus corms. N-terminal amino-acid sequence analysis of the approximately 30?kDa protein showed 33% identity to narbonin, a seed protein from Vicia narbonensis L. The C. vernus chitinase was crystallized by the hanging-drop vapour-diffusion method using PEG 8000 as the main precipitant. The crystal belonged to the monoclinic space group C2, with unit-cell parameters a=172.3, b=37.1, c=126.4?Å, ?=127° and two molecules per asymmetric unit. Diffraction data were collected to a resolution of 2.1?Å.

KW - Animals

KW - Amino Acid Sequence

KW - Molecular Sequence Data

KW - Sequence Alignment

KW - X-Ray Diffraction

KW - Crystallography, X-Ray

KW - Crystallization

KW - Chitinase/chemistry/genetics/isolation & purification

KW - Crocus/enzymology

KW - Globulins/genetics

KW - Vegetable Proteins/genetics

KW - Animals

KW - Amino Acid Sequence

KW - Molecular Sequence Data

KW - Sequence Alignment

KW - X-Ray Diffraction

KW - Crystallography, X-Ray

KW - Crystallization

KW - Chitinase/chemistry/genetics/isolation & purification

KW - Crocus/enzymology

KW - Globulins/genetics

KW - Vegetable Proteins/genetics

M3 - SCORING: Journal article

VL - 67

SP - 340

EP - 343

JO - ACTA CRYSTALLOGR F

JF - ACTA CRYSTALLOGR F

SN - 2053-230X

IS - Pt 3

M1 - Pt 3

ER -