Overproduction, crystallization and preliminary X-ray characterization of Abn2, an endo-1,5-α-arabinanase from Bacillus subtilis
Journal Article
·
· Acta Crystallographica. Section F
- Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Avenida da República-EAN, 2780-157 Oeiras (Portugal)
Native and selenomethionine-derivative Abn2 have been expressed, purified and crystallized. Solution of the selenium substructure allowed the calculation of an initial experimental map at 2.7 Å resolution. Two Bacillus subtilis extracellular endo-1,5-α-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-α-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 Å, α = 82.3, β = 87.9, γ = 63.6°, and P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 57.9, b = 163.3, c = 202.0 Å. X-ray data have been collected for the native and the SeMet derivative to 1.9 and 2.7 Å resolution, respectively. An initial model of Abn2 is being built in the SeMet-phased map.
- OSTI ID:
- 22360583
- Journal Information:
- Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 7 Vol. 64; ISSN ACSFCL; ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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