Purification, crystallization and X-ray diffraction study of basic 7S globulin from soybean

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2011-01, Vol.67 (1), p.87-89
• Main Authors: Yoshizawa, Takuya, Hashimoto, Hiroshi, Shimizu, Toshiyuki, Yamabe, Mayuki, Shichijo, Naoki, Hanada, Kazuki, Hirano, Hisashi, Sato, Mamoru
• Format: Article
• Language: English
• Subjects: Antigens, Plant - chemistry; Antigens, Plant - genetics; Antigens, Plant - isolation & purification; basic 7S globulin; Crystallization; Crystallization Communications; Crystallography; Crystallography, X-Ray; Diffraction; Globulins; Globulins - chemistry; Globulins - genetics; Globulins - isolation & purification; Glycine max - chemistry; Molecular Sequence Data; Purification; Seed Storage Proteins - chemistry; Seed Storage Proteins - genetics; Seed Storage Proteins - isolation & purification; soybean; Soybean Proteins - chemistry; Soybean Proteins - genetics; Soybean Proteins - isolation & purification; Soybeans; X-rays
• ISSN: 1744-3091; 1744-3091; 2053-230X
• DOI: 10.1107/S1744309110046178

Basic 7S globulin (Bg7S) is expressed by soybeans in response to biotic or abiotic stress. Bg7S is capable of binding to a 4 kDa protein which is supposedly involved in cell proliferation. Bg7S is widely found not only in legumes, but also in other plants; however, its function is still unclear. Here, Bg7S was successfully crystallized. Orthorhombic and monoclinic crystals of Bg7S were obtained under different conditions and belonged to space groups P21212, with unit‐cell parameters a = 111.9, b = 130.1, c = 287.8 Å, and P21, with unit‐cell parameters a = 85.3, b = 137.6, c = 162.1 Å, β = 91.2°, respectively.