title: Crystallization and preliminary X-ray structure analysis of pigeon egg-white lysozyme.
abstract: Calcium binding lysozyme from pigeon egg-white was crystallized by the hanging drop vapor diffusion technique using ammonium sulphate as a precipitant. The crystals belong to the orthorhombic system, space group P2(1)2(1)2(1), and have unit cell dimensions of a = 34.2 A, b = 34.8 A, and c = 99.4 A. One asymmetric unit contains one molecule of the pigeon lysozyme. The crystals diffract X-rays at least to 2.0 A resolution and are suitable for high resolution structure analysis. The diffraction data up to 3.0 A resolution were collected with a diffraction image processor, DIP100, using a Fuji imaging plate as an area detector. The structure was solved by the molecular replacement technique and refined to an R factor of 0.216. Least-squares fitting of the main-chains of pigeon egg-white lysozyme with those of chicken egg-white lysozyme and baboon alpha-lactalbumin showed that the main-chain folding of pigeon lysozyme is more similar to that of chicken lysozyme than that of alpha-lactalbumin. The largest differences between the pigeon and chicken lysozymes are in the surface loop regions.
authors.affiliation: Department of Polymer Science, Faculty of Science, Hokkaido University.
authors.forename: M
authors.initials: M
authors.lastname: Yao
authors.forename: I
authors.initials: I
authors.lastname: Tanaka
authors.forename: K
authors.initials: K
authors.lastname: Hikichi
authors.forename: K
authors.initials: K
authors.lastname: Nitta
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism; D002645:Chickens; D010856:Columbidae; D003460:Crystallization; D006801:Humans; D007768:Lactalbumin / Q000737:chemistry*; D008969:Molecular Sequence Data; D009113:Muramidase / Q000737:chemistry*; D014961:X-Ray Diffraction
chemical_list: D007768:Lactalbumin; D009113:Muramidase; D002118:Calcium