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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Expression, purification, crystallization and preliminary crystallographic analysis of an endo-1,5-alpha-L-arabinanase from hyperthermophilic Thermotoga petrophila

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Author(s):
Squina, Fabio Marcio [1] ; Prade, Rolf Alexander [2] ; Wang, Hongliang [2] ; Murakami, Mario Tyago [3]
Total Authors: 4
Affiliation:
[1] Brazilian Assoc Synchrotron Light Technol, Bioethanol Sci & Technol Ctr, BR-13083970 Campinas, SP - Brazil
[2] Oklahoma State Univ, Dept Microbiol & Mol Genet, Stillwater, OK 74078 - USA
[3] Brazilian Assoc Synchrotron Light Technol, Ctr Struct Mol Biol, BR-13083970 Campinas, SP - Brazil
Total Affiliations: 3
Document type: Journal article
Source: ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS; v. 65, n. 9, p. 902-905, Aug. 2009.
Web of Science Citations: 8
Abstract

The endo-1,5-alpha-L-arabinanases belonging to glycoside hydrolase family 43 are of great industrial interest for use in food technology, organic synthesis and biofuel production owing to their ability to catalyze the hydrolysis of alpha-1,5-arabinofuranosidic bonds in arabinose-containing polysaccharides. In this work, Thermotoga petrophila endo-1,5-alpha-L-arabinanase, a GH43-family member, has been cloned, overexpressed, purified and crystallized. Single crystals were obtained from a solution containing 0.1 M MES buffer pH 6.5, 0.8 M ammonium sulfate, 0.1 M EDTA, 0.1 M l-proline and 5%(v/v) dioxane. X-ray diffraction data were collected to a resolution of 2.86 angstrom using synchrotron radiation and the diffraction pattern was indexed in the tetragonal space group P422, with unit-cell parameters a = b = 83.71, c = 408.25 angstrom. (AU)

FAPESP's process: 08/58037-9 - Library generation for biomass-conversion enzymes from soil metagenome
Grantee:Fábio Márcio Squina
Support type: Program for Research on Bioenergy (BIOEN) - Young Investigators Grants