## Abstract

α-L-Arabinofuranosidases (EC 3.2.1.55) are hemicellulases that cleave the glycosidic bond between L-arabinofuranoside side chains and various oligosaccharides. In this study, the first crystallization and preliminary X-ray analysis of the α-L-arabinofuranosidase from Geobacillus stearothermophilus T-6 (AbfA T-6), a family 51 glycoside hydrolase, is described. AbfA T-6 is a hexameric protein consisting of six identical subunits of 502 amino acids and with a calculated molecular mass of 57 218 Da. Purified recombinant native and selenomethionine-containing AbfA T-6 were crystallized by the sitting-drop method in two different space groups, P2_{1} (unit-cell parameters a = 100.8, b = 178.1, c = 196.2 Å, β = 96.1°) and R3 (unit-cell parameters a = b = 179.3, c = 100.4 Å). The R3 crystals diffracted X-rays to a resolution of 1.8 Å.

Original language | English |
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Pages (from-to) | 913-915 |

Number of pages | 3 |

Journal | Acta Crystallographica Section D: Structural Biology |

Volume | 59 |

Issue number | 5 |

DOIs | |

State | Published - 1 May 2003 |

### Bibliographical note

Funding Information:where A is an m x m coefficients' matrix and x and b are vectors of unknowns and right-hand sides, correspondingly. Unfortunately, existing methods may lead to inaccurate solution of (1) where matrix A is ill conditioned, The latter happens rather frequently in physics, engineering, and other branches of science. Solving (1) with standard software, the following warning: "results for solution of ill-conditioned matrix may contain significant numerical error", often appears. The obvious method of overcoming this problem is to scale matrix A appropriately. However, "... the The authors are grateful to Prof. A. Sidi for his interest in the work and useful discussion. This research was supported by the Fund for the Promotion of Research at the Technion.