| CRYSTAL STRUCTURE DETERMINATION OF MUNG BEAN TRYPSIN INHIBITOR Lys FRAGMENT-BOVINE TRYPSIN COMPLEX——MOLECULAR REPLACEMENT,ELECTRON DENSITY MAP AT 3.0 ■ RESOLUTION |
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| 作者姓名： | 曾杰 陈忠国 李根培 卫新成 卢光莹 唐有祺 林光大 张荣光 宣建成 戚正武 曹天钦 |
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| 作者单位： | Institute of Physical Chemistry and Department of Biology，Peking University，Institute of Physical Chemistry and Department of Biology，Peking University，Institute of Physical Chemistry and Department of Biology，Peking University，Institute of Physical Chemistry and Department of Biology，Peking University，Institute of Physical Chemistry and Department of Biology，Peking University，Institute of Physical Chemistry and Department of Biology，Peking University，Shanghai Institute of Biochemistry，Academia Sinica，Shanghai Institute of Biochemistry，Academia Sinica，Shanghai Institute of Biochemistry，Academia Sinica，Shanghai Institute of Biochemistry，Academia Sinica，Shanghai Institute of Biochemistry，Academia Sinica |
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| 基金项目： | Project supported by the National Natural Science Foundation of China. |
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| 摘 要： | The orientation and position of the trypsin molecule in the complex crystal cell mung bean trypsin inhibitor Lys fragment (MBILF)-bovine trypsin (BTRY) have been successfully determined by molecular replacement method with the model of the refined bovine trypsin molecule.Starting from the BTRY coordinates which were oriented and located in the correct azimuth and position in the complex cell according to the result from rotation function and translation function, sim-weighted Fourier map with coefficients 2|F_o|-|F_c| at 3.0 resolution was calculated.Besides the electron density which is obviously attributed to itself, in the vicinity of the active site of BTRY the dense contour levels corresponding to the MBILF and its boundary could be clearly seen in this map. The size of MBILF was approximately estimated at 15×15×25.
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