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Isolation, purification, crystallization and preliminary crystallographic studies of a chitinase fromCrocus vernus
- Source :
- Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67:340-343
- Publication Year :
- 2011
- Publisher :
- International Union of Crystallography (IUCr), 2011.
-
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 A, β = 127° and two molecules per asymmetric unit. Diffraction data were collected to a resolution of 2.1 A.
- Subjects :
- Sequence analysis
Molecular Sequence Data
Biophysics
Sequence alignment
Crystallography, X-Ray
Plant Proteins, Dietary
Biochemistry
law.invention
Crocus vernus
X-Ray Diffraction
Structural Biology
law
Genetics
Animals
Amino Acid Sequence
Crystallization
Peptide sequence
Crocus
biology
Chitinases
food and beverages
Globulins
Condensed Matter Physics
biology.organism_classification
Crystallography
Crystallization Communications
Chitinase
biology.protein
Sequence Alignment
Monoclinic crystal system
Subjects
Details
- ISSN :
- 17443091
- Volume :
- 67
- Database :
- OpenAIRE
- Journal :
- Acta Crystallographica Section F Structural Biology and Crystallization Communications
- Accession number :
- edsair.doi.dedup.....07b55899a7d42b0111f48263df5dfeb9