Document details

Overproduction, crystallization and preliminary X-ray characterization of Abn2,...

Author(s): Sá-Nogueira, Isabel de cv logo 1 ; Sanctis, Daniele de cv logo 2 ; Bento, Isabel cv logo 3 ; Inácio, José Manuel cv logo 4 ; Custódio, Sónia cv logo 5 ; Carrondo, Maria Arménia cv logo 6

Date: 2008

Persistent ID: http://hdl.handle.net/10362/4202

Origin: Repositório Institucional da UNL


Description
Acta Crystallographica F64 (2008) 636-638 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.
Document Type Article
Language English
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