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Expression, purification, crystallization and preliminary X-ray diffraction analysis of Sagittaria sagittifolia

Chunhui Jiang¹, Rui Bao, Yuxing Chen

¹Institute of Protein Research, Tongji University, Shanghai 200092, People's Republic of China.

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications

|November 11, 2008

Abstract:

Protease inhibitors play key roles in physiological processes. Arrowhead protease inhibitor A (API-A), a member of the serine protease inhibitor family, can inhibit two trypsin molecules simultaneously. In the present work, API-A from Sagittaria sagittifolia has been cloned, expressed, purified and crystallized in complex with bovine trypsin. The crystals were obtained by the sitting-drop method. A data set was collected to 2.48 A resolution from a single crystal. The crystal belonged to space group C222(1), with unit-cell parameters a = 76.63, b = 110.86, c = 152.99 A, alpha = beta = gamma = 90 degrees .

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