Crystallization and preliminary X-ray analysis of a thermostable pectate lyase PL 47 from Bacillus sp. TS 47.
The thermostable pectate lyase PL 47 from Bacillus sp. TS 47, with a molecular weight of 50 kDa, was crystallized by the hanging-drop vapour-diffusion method using 2-propanol and polyethylene glycol 4000 as precipitants. The crystals belong to the trigonal space group P3(1)21, with unit-cell parameters a = b = 58.8, c = 229.7 A, gamma = 120 degrees. The calculated V(M) based on one molecule per asymmetric unit is 2.30 A(3) Da(-1). A native data set from a frozen crystal was collected to 1.8 A resolution using synchrotron radiation at SPring-8. A molecular-replacement solution was obtained using the structure of pectate lyase from B. subtilis as a model.
Nakaniwa
Tetsuko
T
Research Institute for Advanced Science and Technology, Osaka Prefecture University, Sakai, Osaka 599-8570, Japan. tetsuko@riast.osakafu-u.ac.jp
Tada
Toshiji
T
Ishii
Keiko
K
Takao
Makoto
M
Sakai
Takuo
T
Nishimura
Keiichiro
K
D001407:Bacillus / Q000201:enzymology*; D003460:Crystallization / Q000379:methods; D018360:Crystallography, X-Ray; D004795:Enzyme Stability; D006358:Hot Temperature; D011133:Polysaccharide-Lyases / Q000737:chemistry* / Q000235:genetics; D017356:Synchrotrons
D011133:Polysaccharide-Lyases; C023911:pectate lyase