Davydova N, Fedorov R, Streltsov V, Liljas A, Garber M
Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia.
Acta Crystallogr D Biol Crystallogr. 2001 Aug;57(Pt 8):1150-2. doi: 10.1107/s090744490100868x. Epub 2001 Jul 23.
A mutant form of Thermus thermophilus ribosomal protein L22 responsible for erythromycin resistance has been overexpressed in Escherichia coli, purified to homogeneity and crystallized using the hanging-drop vapour-diffusion technique. While several different crystallization conditions were found, only one set of conditions yielded crystals suitable for X-ray diffraction analysis. These crystals grow as thick plates, with unit-cell parameters a = 31.8, b = 86.59, c = 38.96 A, beta = 104.47 degrees. The crystals belong to the space group P2(1) and diffract to 1.8 A resolution. On the basis of density calculations, two monomers are predicted per asymmetric unit (V(M) = 2.06 A(3) Da(-1)), with a solvent content of 40%.
一种负责红霉素抗性的嗜热栖热放线菌核糖体蛋白L22的突变形式已在大肠杆菌中过表达,纯化至同质,并使用悬滴气相扩散技术进行结晶。虽然发现了几种不同的结晶条件,但只有一组条件产生了适合X射线衍射分析的晶体。这些晶体生长为厚板,晶胞参数a = 31.8,b = 86.59,c = 38.96 Å,β = 104.47°。晶体属于空间群P2(1),衍射分辨率为1.8 Å。基于密度计算,每个不对称单元预测有两个单体(V(M)=2.06 ų Da⁻¹),溶剂含量为40%。