title: Crystallization, X-ray diffraction analysis and SIRAS phasing of human α-L-iduronidase.
abstract: Human lysosomal α-L-iduronidase, whose deficiency causes mucopolysaccharidosis type I, was crystallized using sodium/potassium tartrate and polyethylene glycol 3350 as a precipitant. Using synchrotron radiation, a native data set was collected from a single crystal at 100 K to 2.3 Å resolution. The crystal belonged to space group R3 with unit-cell dimensions of a=b=259.22, c=71.83 Å. To obtain the phase information, mercury-derivative crystals were prepared and a single-wavelength anomalous dispersion (SAD) data set was collected at the Hg peak wavelength. Phase calculation with the single isomorphous replacement with anomalous scattering (SIRAS) method successfully yielded an interpretable electron-density map.
authors.affiliation: Laboratory of X-ray Crystallography, Institute for Enzyme Research, University of Tokushima, 3-18-15, Kuramotocho, Tokushima 770-8503, Japan. nmaita@tokushima-u.ac.jp
authors.forename: Nobuo
authors.initials: N
authors.lastname: Maita
authors.forename: Hisaaki
authors.initials: H
authors.lastname: Taniguchi
authors.forename: Hitoshi
authors.initials: H
authors.lastname: Sakuraba
mesh_terms: D000818:Animals; D016466:CHO Cells; D006224:Cricetinae; D003460:Crystallization; D006801:Humans; D007068:Iduronidase / Q000737:chemistry*; D008628:Mercury / Q000737:chemistry; D014961:X-Ray Diffraction / Q000379:methods
chemical_list: D007068:Iduronidase; D008628:Mercury