Archaeal acylamino acid releasing enzyme/lipase:Crystallization and preliminary crystallographic analysis in a new crystal form  

作　　者：WANGGanggang GAORenjun 等 

机构地区：[1]MOELaboratoryofProteinScience&LaboratoryofStructuralBiology.DepartmentofBiologicalScienceandBiotechnology,TsinghuaUniversity.Beijing,100084.China [2]KeyLaboratoryforMolecularEnzymolo

出　　处：《Chinese Science Bulletin》2003年第2期154-155,共2页

基　　金：This work was supported by the 73 Project (Grant No. G1999075602).

摘　　要：A primitive orthorhombic crystal form of acylamino acid releasing enzyme/lipase (APE1547) from hyperthermophilic archaeon Aeropyrum pernix strain K1 has been obtained at 291 K. The diffraction pattern of the crystal extends to 0.27 nm resolution at 100 K using Cu Ka radiation. The crystal belongs to the space group P212121 with unit cell dimensions of a = 6.399, b = 10.439 and c = 16.953 nm. The presence of two molecules per asymmetric unit gives a crys-tal volume per protein mass (Vm) of 0.0022 nm3 Da-1 and a solvent content of 43% by volume. A full set of X-ray dif-fraction data were collected to 0.3 nm from the native crys-tal.A primitive orthorhombic crystal form of acylamino acid releasing enzyme/lipase (APE1547) from hyperthermophilic archaeon Aeropyrum pernix strain K1 has been obtained at 291 K. The diffraction pattern of the crystal extends to 0.27 nm resolution at 100 K using Cu Ka radiation. The crystal belongs to the space group P212121 with unit cell dimensions of a = 6.399, b = 10.439 and c = 16.953 nm. The presence of two molecules per asymmetric unit gives a crys-tal volume per protein mass (Vm) of 0.0022 nm3 Da-1 and a solvent content of 43% by volume. A full set of X-ray dif-fraction data were collected to 0.3 nm from the native crys-tal.

关 键 词：古细胞 脂肪酶 结晶形成 晶体结构分析 酰基肽水解酶 

分 类 号：Q936[生物学—微生物学] Q933