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.
Tada
T
T
Research Institute for Advanced Science and Technology, Osaka Prefecture University, Sakai, Osaka 599-8570, Japan. tada@riast.osakafu-u.ac.jp
Lu
C T
CT
Nakamura
Y
Y
Wada
K
K
Miyahara
I
I
Hirotsu
K
K
Katsuya
Y
Y
Sawada
M
M
Takao
M
M
Sakai
T
T
Nishimura
K
K
D003460:Crystallization; D018360:Crystallography, X-Ray; D011133:Polysaccharide-Lyases / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D014250:Trichosporon / Q000201:enzymology*
D011133:Polysaccharide-Lyases; C027349:pectin lyase