Abstract
The alpha-1,6-fucosyltransferase NodZ from Bradyrhizobium sp. WM9 (Lupinus), composed of 325 amino acids with a molecular weight of 37 kDa, has been cloned, expressed and purified. Protein crystals suitable for X-ray diffraction were obtained under optimized crystallization conditions using ammonium dihydrogen phosphate as a precipitant. The crystals are hexagonal and belong to space group P6(1)22 or P6(5)22, with unit-cell parameters a = 125.5, c = 95.6 A, and contain 56.8% solvent and a single protein molecule in the asymmetric unit. Native data were collected to 2.85 A using synchrotron radiation and cryogenic conditions. The native crystals were soaked in a mother-liquor solution containing 2.5 mM [Ta(6)Br(12)](2+) cluster for derivatization and SAD data were collected to 3.4 A at the tantalum L(III) absorption peak.
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Schedule a callMore From: Acta crystallographica. Section D, Biological crystallography
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