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Crystallization, X-ray diffraction analysis and SIRAS phasing of human ?-L-iduronidase.

ABSTRACT: Human lysosomal ?-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.

SUBMITTER: Maita N

PROVIDER: S-EPMC3515382 | biostudies-literature | 2012 Nov

REPOSITORIES: biostudies-literature

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Crystallization, X-ray diffraction analysis and SIRAS phasing of human α-L-iduronidase.

Maita Nobuo N Taniguchi Hisaaki H Sakuraba Hitoshi H

Acta crystallographica. Section F, Structural biology and crystallization communications 20121030 Pt 11

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 disp ...[more]

PMID: 23143250

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