Hakim Aaron, Thakral Durga, Zhu Darren F, Nguyen Jennifer B
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 May 1;68(Pt 5):547-50. doi: 10.1107/S1744309112010421. Epub 2012 Apr 20.
Antifreeze proteins (AFPs) are a specialized evolutionary adaptation of a variety of bacteria, fish, arthropods and other organisms to inhibit ice-crystal growth for survival in harsh subzero environments. The recently reported novel hyperactive AFP from Rhagium inquisitor (RiAFP) is the second distinct type of AFP in beetles and its structure could reveal important molecular insights into the evolution of AFPs. For this purpose, RiAFP was overexpressed in Escherichia coli, purified and crystallized at 293 K using a combination of 23% PEG 3350 and 0.2 M ammonium sulfate as a precipitant. X-ray diffraction data were collected to 1.3 Å resolution using a synchrotron-radiation source. The crystals belonged to the trigonal space group P3(1)21 (or P3(2)21), with unit-cell parameters a = b = 46.46, c = 193.21 Å.
抗冻蛋白（AFPs）是多种细菌、鱼类、节肢动物和其他生物的一种特殊进化适应性产物，可抑制冰晶生长，以便在严寒的零下环境中生存。最近报道的来自长角窃蠹（RiAFP）的新型高活性抗冻蛋白是甲虫体内第二种不同类型的抗冻蛋白，其结构可能揭示抗冻蛋白进化的重要分子见解。为此，RiAFP在大肠杆菌中过表达，使用23% PEG 3350和0.2 M硫酸铵的组合作为沉淀剂在293 K下进行纯化和结晶。使用同步辐射源收集了分辨率为1.3 Å的X射线衍射数据。晶体属于三方空间群P3(1)21（或P3(2)21），晶胞参数a = b = 46.46，c = 193.21 Å。
