@article {deSanctis:bw5242, title = {Overproduction, crystallization and preliminary X-ray characterization of Abn2, an endo-1,5-α-arabinanase from Bacillus subtilis}, journal = {Acta Crystallographica Section F}, volume = {64}, number = {7}, year = {2008}, note = {

n/a

}, pages = {636{\textendash}638}, abstract = {

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 {\r A}, α = 82.3, β = 87.9, ɣ = 63.6{\textdegree}, and P212121, with unit-cell parameters a = 57.9, b = 163.3, c = 202.0 {\r A}. X-ray data have been collected for the native and the SeMet derivative to 1.9 and 2.7 {\r A} resolution, respectively. An initial model of Abn2 is being built in the SeMet-phased map.

}, doi = {10.1107/S1744309108016321}, author = {de Sanctis, Daniele and Bento, Isabel and In{\'a}cio, Jos{\'e} Manuel and Cust{\'o}dio, S{\'o}nia and Isabel de S{\'a}-Nogueira and Carrondo, Maria Arm{\'e}nia} }