Expression, purification, crystallization and preliminary X-ray diffraction analysis of Sagittaria sagittifolia arrowhead protease inhibitor API-A in complex with bovine trypsin.
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 .
Jiang
Chunhui
C
Institute of Protein Research, Tongji University, Shanghai 200092, People's Republic of China.
Bao
Rui
R
Chen
Yuxing
Y
D000818:Animals; D002417:Cattle; D003460:Crystallization; D008969:Molecular Sequence Data; D046912:Multiprotein Complexes / Q000737:chemistry; D010940:Plant Proteins / Q000737:chemistry*; D011480:Protease Inhibitors / Q000737:chemistry*; D011487:Protein Conformation; D034903:Sagittaria / Q000737:chemistry*; D014357:Trypsin / Q000737:chemistry; D014961:X-Ray Diffraction
C080655:API-A protein, Sagittaria sagittifolia; D046912:Multiprotein Complexes; D010940:Plant Proteins; D011480:Protease Inhibitors; D014357:Trypsin