Derrick J P, Feavers I, Maiden M C
Department of Biomolecular Sciences, UMIST, Manchester M60 lQD, England.
Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):314-6. doi: 10.1107/S0907444998010269. Epub 1999 Jan 1.
Crystals have been obtained of an antibody Fab fragment grown in the presence of a single domain from streptococcal protein G and a ten amino-acid peptide corresponding to the P1.7 serosubtype antigen from the human pathogen Neisseria meningitidis. Crystal trials using the Fab fragment and peptide antigen alone were unsuccessful, but the inclusion of a protein G domain provided an additional variable that generated suitable crystals. Crystals are in space group P21 with unit-cell parameters a = 43.60, b = 63.42, c = 89.63 A, beta = 98.58 degrees and a data set has been collected to 2.9 A resolution using synchrotron radiation. The inclusion of protein G is likely to be of general utility for the crystallization of Fab-antigen complexes.
在来自链球菌蛋白G的单个结构域和对应于人病原体脑膜炎奈瑟菌P1.7血清亚型抗原的十氨基酸肽存在的情况下生长的抗体Fab片段已获得晶体。单独使用Fab片段和肽抗原进行的晶体筛选未成功，但加入蛋白G结构域提供了一个额外变量，从而产生了合适的晶体。晶体属于空间群P21，晶胞参数为a = 43.60、b = 63.42、c = 89.63 Å、β = 98.58°，并且使用同步辐射已收集到分辨率为2.9 Å的数据集。加入蛋白G可能对Fab-抗原复合物的结晶具有普遍用途。
