Purification, crystallization and preliminary X-ray diffraction analysis of the fructose-1,6-/sedoheptulose-1,7-bisphosphatase of Synechococcus PCC 7942.

Fructose-1,6-/sedoheptulose-1,7-bisphosphatase of Synechococcus PCC 7942, overexpressed from Escherichia coli, has been purified and crystallized by the hanging-drop vapour-diffusion method using ammonium sulfate as a precipitant. The crystals were monoclinic, with unit-cell parameters a = 80.1, b = 84.2, c = 104.3 A, beta = 101.7 degrees. They belonged to space group P2(1) and diffracted to at least 2.2 A resolution. The calculated V(M) value, based on a tetramer in the asymmetric unit, was 2.2 A(3) Da(-1).

Crystallization and preliminary X-ray analysis of a novel pectolytic enzyme, polymethoxygalacturonase SX1 from Trichosporon penicillatum.

A novel pectolytic enzyme, polymethoxygalacturonase SX1 from Trichosporon penicillatum, with a molecular weight of 36 kDa was crystallized by the hanging-drop vapour-diffusion method using polyethylene glycol 1000 as a precipitant. The crystals belonged to the monoclinic space group C2, with unit-cell parameters a = 165.6, b = 61.0, c = 48.7 A, beta = 93.1 degrees. The calculated V(M) based on one molecule per asymmetric unit was 3.40 A(3) Da(-1). A native data set was collected to 2.08 A resolution from a crystal on a Cu Kalpha rotating-anode X-ray source. A molecular-replacement solution was obtained using the program AMoRe and the structure of endopolygalacturonase II from Aspergillus niger as a model.