T. Tada et al., Crystallization and preliminary X-ray analysis of a novel pectolytic enzyme, polymethoxygalacturonase SX1 from Trichosporon penicillatum, ACT CRYST D, 57, 2001, pp. 457-458
A novel pectolytic enzyme, polymethoxygalacturonase SX1 from Trichosporon p
enicillatum, with a molcular weight of 36 kDa was crystallized by the hangi
ng-drop vapour-diffusion method using polyethylene glycol 1000 as a precipi
tant. The crystals belonged to the monoclinic space group C2, with unit-cel
l parameters a = 165.6, b = 61.0, c = 48.7 Angstrom, beta = 93.1 degrees. T
he calculated V-M based on one molecule per asymmetric unit was 3.40 Angstr
om (3) Da(-1). A native data set was collected to 2.08 Angstrom resolution
from a crystal on a Cu K alpha rotating-anode X-ray source. A molecular-rep
lacement solution was obtained using the program AMoRe and the structure of
endopolygalacturonase II from Aspergillus niger as a model.