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

Citation
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
Citations number
23
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
57
Year of publication
2001
Part
3
Pages
457 - 458
Database
ISI
SICI code
0907-4449(200103)57:<457:CAPXAO>2.0.ZU;2-P
Abstract
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.