Crystallization and preliminary crystallographic analysis of endo-1,3-beta-glucanase from alkaliphilic Nocardiopsis sp. strain F96
| Autor: | Takashi Kumasaka, Satoshi Nakamura, Raita Hirose, Guntur Fibriansah, Nobuo Tanaka, Kensaku Hamada, Sumiko Masuda |
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| Rok vydání: | 2005 |
| Předmět: |
Biophysics
Crystallography X-Ray Biochemistry law.invention Hydrolysis Bacterial Proteins Structural Biology law Actinomycetales Genetics Glycoside hydrolase Crystallization Glucan chemistry.chemical_classification biology Glucan Endo-1 3-beta-D-Glucosidase Space group Glucanase Condensed Matter Physics biology.organism_classification Recombinant Proteins Crystallography chemistry Crystallization Communications Bacteria |
| Zdroj: | Acta crystallographica. Section F, Structural biology and crystallization communications. 62(Pt 1) |
| ISSN: | 1744-3091 |
| Popis: | Endo-1,3-beta-glucanase, an enzyme that hydrolyzes the 1,3-beta-glycosyl linkages of beta-glucan, belongs to the family 16 glycosyl hydrolases, which are widely distributed among bacteria, fungi and higher plants. Crystals of a family 16 endo-1,3-beta-glucanase from the alkaliphilic Nocardiopsis sp. strain F96 were obtained by the hanging-drop vapour-diffusion method. The crystals belonged to space group P2(1), with unit-cell parameters a = 34.59, b = 71.84, c = 39.67 A, beta = 90.21 degrees, and contained one molecule per asymmetric unit. The Matthews coefficient (VM) and solvent content were 1.8 A3 Da(-1) and 31.8%, respectively. Diffraction data were collected to a resolution of 1.3 A and gave a data set with an overall Rmerge of 6.4% and a completeness of 99.3%. |
| Databáze: | OpenAIRE |
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