Triclinic lysozyme at 0.65 Å resolution
Triclinic lysozyme at 0.65 Å resolution
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DOI：
10.1107/s0907444907054224
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发表时间：
2007-12-01
影响因子：
2.2
通讯作者：
Dauter, Zbigniew
中科院分区：
文献类型：
--
作者：
Wang, Jiawei;Dauter, Miroslawa;Dauter, Zbigniew
三斜晶系鸡蛋清溶菌酶（HEWL）的晶体结构已被细化对衍射数据扩展到0.65埃分辨率在100 K测量使用同步辐射。与各向异性位移参数和消除立体化学约束的结构的有序部分收敛与传统的R因子为8.39%和R-自由的9.52%。使用全矩阵细化提供了推导参数的方差估计值。除了129个残基的蛋白质，总共170个水分子，9个硝酸根离子，1个乙酸根离子和3个乙二醇分子位于电子密度图中。主链的八个部分和许多侧链被建模为具有交替构象。水站点的占用率进行了细化，这一步骤是有意义的，当使用的自由R因子进行评估。参考先前报道的在0.925埃（在120 K的低温下）和在0.95埃分辨率（在室温下）下精制的三斜HEWL结构，对结构进行详细描述和比较。
The crystal structure of triclinic hen egg-white lysozyme (HEWL) has been refined against diffraction data extending to 0.65 angstrom resolution measured at 100 K using synchrotron radiation. Refinement with anisotropic displacement parameters and with the removal of stereochemical restraints for the well ordered parts of the structure converged with a conventional R factor of 8.39% and an R-free of 9.52%. The use of full-matrix refinement provided an estimate of the variances in the derived parameters. In addition to the 129-residue protein, a total of 170 water molecules, nine nitrate ions, one acetate ion and three ethylene glycol molecules were located in the electron-density map. Eight sections of the main chain and many side chains were modeled with alternate conformations. The occupancies of the water sites were refined and this step is meaningful when assessed by use of the free R factor. A detailed description and comparison of the structure are made with reference to the previously reported triclinic HEWL structures refined at 0.925 angstrom (at the low temperature of 120 K) and at 0.95 angstrom resolution (at room temperature).