Crystallization and preliminary X-ray crystallographic analysis of S-allelic glycoprotein S(F11)-RNase from Nicotiana alata.
Nicotiana alata S(F11)-RNase is an S-glycoprotein associated with gametophytic self-incompatibility. Crystals of S(F11)-RNase have been grown at room temperature using polyethylene glycol as a precipitant. A crystal diffracted to better than 1.4 A resolution at 100 K at the SPring-8 synchrotron-radiation source, indicating that it is very suitable for high-resolution structure analysis. The crystal belongs to the space group P2(1), with unit-cell parameters a = 65.86 (11), b = 44.73 (5), c = 64.36 (7) A, beta = 90.27 (9) degrees. The asymmetric unit contains two monomers, giving a crystal volume per protein mass (V(M)) of 2.05 A(3) Da(-1) and a solvent content of 39.6% by volume. A full set of X-ray diffraction data was collected to 1.55 A resolution with a completeness of 97.4%. A heavy-atom derivative has been successfully prepared with ethylmercury thiosalicylate (EMTS) and structure analysis is in progress.
Ida
K
K
Graduate School of Integrated Science, Yokohama City University, Kanazawa-ku, Yokohama 236-0027, Japan.
Shinkawa
T
T
Norioka
S
S
Newbigin
E
E
Clarke
A E
AE
Sakiyama
F
F
Sato
M
M
D003460:Crystallization; D018360:Crystallography, X-Ray; D010947:Plants, Toxic; D011487:Protein Conformation; D012260:Ribonucleases / Q000737:chemistry*; D014026:Nicotiana / Q000201:enzymology*
D012260:Ribonucleases