慈姑箭头蛋白酶抑制剂API-A与牛胰蛋白酶复合物的表达、纯化、结晶及初步X射线衍射分析
Expression, purification, crystallization and preliminary X-ray diffraction analysis of Sagittaria sagittifolia arrowhead protease inhibitor API-A in complex with bovine trypsin.
作者信息
Jiang Chunhui, Bao Rui, Chen Yuxing
机构信息
Institute of Protein Research, Tongji University, Shanghai 200092, People's Republic of China.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Nov 1;64(Pt 11):1060-2. doi: 10.1107/S1744309108032454. Epub 2008 Oct 31.
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 .
摘要
蛋白酶抑制剂在生理过程中发挥着关键作用。慈菇蛋白酶抑制剂A（API-A）是丝氨酸蛋白酶抑制剂家族的成员之一，能够同时抑制两个胰蛋白酶分子。在本研究中，已从慈姑中克隆、表达、纯化了API-A，并使其与牛胰蛋白酶形成复合物进行结晶。晶体通过坐滴法获得。从单晶收集到分辨率为2.48 Å的数据集。该晶体属于空间群C222(1)，晶胞参数为a = 76.63，b = 110.86，c = 152.99 Å，α = β = γ = 90°。
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