CRYSTALLIZATION AND PRELIMINARY-X-RAY STUDIES OF RHAMNOGALACTURONASE-A FROM ASPERGILLUS-ACULEATUS

Recombinant rhamnogalacturonase A from Aspergillus aculeatus has been crystallized and X-ray diffraction data has been collected. Crystals w ere grown by the hanging-drop vapour-diffusion technique, under the co nditions 10% PEG 8000, 0.05 M KH2PO4 and 0.1 M sodium acetate buffered at pH 3.5. The crystals diffract beyond 2.0 Angstrom resolution and b elong to one of the orthorhombic space groups I2(1)2(1)2(1) or I222, w ith the unit-cell parameters a = 62.9, b = 125.4 and c = 137.0 Angstro m. There is one molecule in the asymmetric unit and a solvent content of approximately 54%. The enzyme is highly glycosylated corresponding to 5.9 kDa.