title: Triclinic lysozyme at 0.65 A resolution.
abstract: The crystal structure of triclinic hen egg-white lysozyme (HEWL) has been refined against diffraction data extending to 0.65 A 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 A (at the low temperature of 120 K) and at 0.95 A resolution (at room temperature).
authors: SAIC-Frederick Inc., Basic Research Program, Argonne National Laboratory, Argonne, IL 60439, USA.
authors: Jiawei
authors: J
authors: Wang
authors: Miroslawa
authors: M
authors: Dauter
authors: Randy
authors: R
authors: Alkire
authors: Andrzej
authors: A
authors: Joachimiak
authors: Zbigniew
authors: Z
authors: Dauter
mesh_terms: D000818:Animals; D016880:Anisotropy; D020134:Catalytic Domain; D002642:Chick Embryo; D003460:Crystallization; D018360:Crystallography, X-Ray; D016018:Least-Squares Analysis; D008958:Models, Molecular; D009113:Muramidase / Q000737:chemistry*; D011487:Protein Conformation; D054159:Torsion, Mechanical
chemical_list: C421864:hen egg lysozyme; D009113:Muramidase