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期刊论文
Crystallization and preliminary X-ray analysis of an alkaline serine protease from Nesterenkonia sp.
Acta Cryst. (2003). D59, 529-531，-0001，（）：
A novel calcium-independent serine protease from an alkaliphilic bacterium, Nesterenkonia sp. AL20, has been purified and crystallized at 296 Kusing 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
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