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Please use this identifier to cite or link to this item: http://hdl.handle.net/10362/4202

Title: Overproduction, crystallization and preliminary X-ray characterization of Abn2, an endo-1,5-alpha-arabinanase from Bacillus subtilis.
Authors: Sá-Nogueira, Isabel de
Sanctis, Daniele de
Bento, Isabel
Inácio, José Manuel
Custódio, Sónia
Carrondo, Maria Arménia
Issue Date: 2008
Publisher: International Union of Crystallography
Citation: de Sanctis D, Bento I, Inácio JM, Custódio S, de Sá-Nogueira I, and Carrondo MA (2008). Overproduction, crystallization and preliminary X-ray characterization of Abn2, an endo-1,5-alpha-arabinanase from Bacillus subtilis. Acta Crystallogr Sect F Struct Biol Cryst Commun. 64(Pt 7):636-638.
Abstract: Two Bacillus subtilis extracellular endo-1,5-alpha-L-arabinanases, AbnA and Abn2, belonging to glycoside hydrolase family 43 have been identified. The recently characterized Abn2 protein hydrolyzes arabinan and has low identity to other reported 1,5-alpha-L-arabinanases. Abn2 and its selenomethionine (SeMet) derivative have been purified and crystallized. Crystals appeared in two different space groups: P1, with unit-cell parameters a = 51.9, b = 57.6, c = 86.2 A, alpha = 82.3, beta = 87.9, gamma = 63.6 degrees , and P2(1)2(1)2(1), with unit-cell parameters a = 57.9, b = 163.3, c = 202.0 A. X-ray data have been collected for the native and the SeMet derivative to 1.9 and 2.7 A resolution, respectively. An initial model of Abn2 is being built in the SeMet-phased map.
Description: Acta Crystallographica F64 (2008) 636-638
URI: http://hdl.handle.net/10362/4202
ISSN: 1744-3091
Appears in Collections:FCT: DCV - Artigos em revista internacional com arbitragem científica

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