Strelkov S V, Zurabishvili T G, Nepluev I V, Efimov V P, Isupov M N, Harutyunyan E H, Mesyanzhinov V V
Ivanovsky Institute of Virology, Moscow, Russia.
J Mol Biol. 1993 Nov 20;234(2):493-5. doi: 10.1006/jmbi.1993.1601.
The structural protein, gene product 9 (gp9), of bacteriophage T4 controls baseplate expansion at the first steps of virus attachment onto its host bacterial cell with subsequent tail contraction. Gp9, which has an M(r) of 30.8 kDa and contains 287 amino acids, has been purified from a recombinant Escherichia coli strain and crystallized at 25 degrees C using the hanging drop vapor diffusion method at pH 4.0 with ammonium sulfate as precipitant. The crystals of gp9 belong to the space group R32 with hexagonal cell dimensions a = b = 86.5 A and c = 156.2 A and diffract X-rays to at least 2.7 A. There is one molecule per asymmetric unit.
噬菌体T4的结构蛋白基因产物9（gp9）在病毒附着于宿主细菌细胞的最初阶段控制基板扩张，随后尾部收缩。gp9的相对分子质量为30.8 kDa，含有287个氨基酸，已从重组大肠杆菌菌株中纯化出来，并于25℃使用悬滴气相扩散法，在pH 4.0、以硫酸铵作为沉淀剂的条件下结晶。gp9晶体属于空间群R32，六方晶胞参数a = b = 86.5 Å，c = 156.2 Å，X射线衍射分辨率至少为2.7 Å。每个不对称单元中有一个分子。
