Crystallization and preliminary X-ray analysis of an alkaline serine protease from Nesterenkonia sp.
A novel calcium-independent serine protease from an alkaliphilic bacterium, Nesterenkonia sp. AL20, has been purified and crystallized at 296 K using sodium formate as the main precipitant. This enzyme is optimally active at pH 10, exhibits high stability towards autolytic digestion and its stability is not affected by the presence of EDTA or detergents. The triangular prism-shaped crystals diffracted X-rays to beyond 1.5 A at a synchrotron beamline, with space group R3 and unit-cell parameters a = b = 92.26, c = 137.88 A. A complete data set has been collected to 1.39 A resolution. The asymmetric unit is estimated and confirmed by self-rotation function calculation to contain two molecules, giving a crystal Volume per protein mass (V(M)) of 2.68 A(3) Da(-1) and a solvent content of 54%.
Bakhtiar
Shahrzad
S
Department of Biotechnology, Center for Chemistry and Chemical Engineering, Lund University, S-221 00 Lund, Sweden.
Vévodová
Jitka
J
Hatti-Kaul
Rajni
R
Su
Xiao Dong
XD
D000192:Actinomycetales / Q000201:enzymology*; D003460:Crystallization; D006868:Hydrolysis; D008958:Models, Molecular; D012697:Serine Endopeptidases / Q000032:analysis / Q000737:chemistry* / Q000302:isolation & purification
D012697:Serine Endopeptidases