CRYSTALLIZATION AND PRELIMINARY-X-RAY STUDIES ON CANDIDA-CYLINDRACEA LIPASE

As part of the programme to understand the mechanism and specificity o f lipase enzymes used in biotransformation reactions, the lipase from Candida cylindracea has been purified and crystallized. This lipase ha s been widely used by organic chemists for hydrolysis and esterificati on reactions. Crystals were obtained using polyethylene glycol 6000 as a precipitant and grew to 0.6 mm in the maximum dimension. The enzyme crystallized in the space group P2(1) with unit-cell dimensions a=94. 3, b=117.0, and c=114.2 Angstrom with beta=109.2 degrees. Calculations indicate that there are four molecules in the asymmetric unit. The cr ystals diffract to at least 2.5 Angstrom resolution and the structure has been solved by molecular replacement using the lipase from Geotric hum candidum as a search model.