Crystallization and preliminary crystallographic studies of the Pasteurella multocida toxin catalytic domain.
The C-terminal catalytic domain of Pasteurella multocida toxin, which is the virulence factor of the organism in P. multocida, has been expressed, purified and subsequently crystallized using the sitting-drop vapour-diffusion technique. Native diffraction data to 1.9 A resolution were obtained at the BL44XU beamline of SPring-8 from a flash-frozen crystal at 100 K. The crystals belong to space group C2, with unit-cell parameters a = 111.0, b = 150.4, c = 77.1 A, beta = 105.5 degrees, and are likely to contain one C-PMT (726 residues) per asymmetric unit.
Miyazawa
Masayuki
M
Research Institute for Microbial Diseases, Osaka University, 3-1 Yamada-oka, Suita-shi, Osaka 565-0871, Japan.
Kitadokoro
Kengo
K
Kamitani
Shigeki
S
Shime
Hiroaki
H
Horiguchi
Yasuhiko
Y
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D001427:Bacterial Toxins / Q000737:chemistry*; D020134:Catalytic Domain; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D008969:Molecular Sequence Data; D016979:Pasteurella multocida / Q000737:chemistry* / Q000472:pathogenicity; D037521:Virulence Factors / Q000737:chemistry / Q000235:genetics
D001426:Bacterial Proteins; D001427:Bacterial Toxins; C062258:Pasteurella multocida toxin; D037521:Virulence Factors