Abstract
CrChi1 is a chitinase from the nematophagous fungus Clonostachys rosea that plays a role in the infection of nematodes. In order to resolve the crystal structure of CrChi1 and to gain a better understanding of its biological functions, recombinant CrChi1 was crystallized at 291 K using PEG 3350 and ammonium dihydrogen phosphate as precipitant and a 1.8 A resolution X-ray data set was collected from a single flash-cooled crystal (100 K). The crystals belonged to space group P2(1), with unit-cell parameters a = 44.1, b = 71.7, c = 59.1 A, alpha = gamma = 90, beta = 91.3 degrees. Assuming the presence of one molecule per asymmetric unit, the Matthews coefficient and solvent content were calculated to be 2.45 A(3) Da(-1) and 40%, respectively. To our knowledge, this is the first structure determination study of a chitinase from a nematophagous fungus.