AN X-RAY ANALYSIS OF THE ORTHORHOMBIC CRYSTAL FORM OF TRICHOSANTHIN AT 5

• 作 者: 马星奇 王耀萍 王家槐
• 机 构: Institute of Biophysics, Academia Sinica, Beijing,Institute of Biophysics, Academia Sinica, Beijing,
• 出 处: Science in China,Ser.B
• 发表日期: 1987年07期
• 关键词: residues preliminary conformational alkali FORM dramatic orthorhombic asymmetric

Trichosanthin crystals grown at pH 5.4 are orthorhombic P2_12_12_1 with cell dimension α=38.23, b=76.18 and c=79.12. Each asymmetric unit contains one protein molecule of 234 amino acid residues (M. W. 26,000). The structure has been solved at 5 resolution by conventional MIR method with two heavy-atom derivatives. The preliminary result suggests that the protein molecule in acidic solution does not have dramatic conformational change, compared with that in alkali solution.

Trichosanthin crystals grown at pH 5.4 are orthorhombic P2_12_12_1 with cell dimension α = 38.23, b = 76.18 and c = 79.12. The asymmetry unit contains one protein molecule of 234 amino acid residues (MW 26,000). The structure has been solved at 5 resolution by conventional MIR method with two heavy-atom derivatives. The preliminary result suggests that the protein molecule in acidic solution does not have dramatic conformational change, compared with that in alkali solution.