细菌表达的抗溶菌酶单克隆抗体D1.3的Fv片段及其与抗原溶菌酶复合物的结晶和初步X射线衍射研究。
Crystallization and preliminary X-ray diffraction study of the bacterially expressed Fv from the monoclonal anti-lysozyme antibody D1.3 and of its complex with the antigen, lysozyme.
作者信息
Boulot G, Eiselé J L, Bentley G A, Bhat T N, Ward E S, Winter G, Poljak R J
机构信息
U.R.A. 359 C.N.R.S., Département d'Immunologie, Institut Pasteur, Paris, France.
出版信息
J Mol Biol. 1990 Jun 20;213(4):617-9. doi: 10.1016/S0022-2836(05)80248-7.
The associated heavy (VH) and light (VL) chain variable domains (Fv) of the monoclonal anti-lysozyme antibody D1.3, secreted from Escherichia coli, have been crystallized in their antigen-bound and free forms. FvD1.3 gives tetragonal crystals, space group P4(1)2(1)2 (or P4(3)2(1)2), with a = 90.6 A, c = 56.4 A. The FvD1.3-lysozyme complex crystallizes in space group C2, with a = 129.2 A, b = 60.8 A, c = 56.9 A and beta = 119.3 degrees. The crystals contain one molecule of Fv or of the Fv-lysozyme complex in their asymmetric units and diffract X-rays to high resolution, making them suitable for X-ray crystallographic studies.
从大肠杆菌分泌的单克隆抗溶菌酶抗体D1.3的相关重链（VH）和轻链（VL）可变结构域（Fv），已分别以与抗原结合及游离的形式结晶。FvD1.3形成四方晶体，空间群为P4(1)2(1)2（或P4(3)2(1)2），a = 90.6 Å，c = 56.4 Å。FvD1.3-溶菌酶复合物结晶于空间群C2中，a = 129.2 Å，b = 60.8 Å，c = 56.9 Å，β = 119.3°。这些晶体在其不对称单元中含有一个Fv分子或Fv-溶菌酶复合物分子，并且能将X射线衍射至高分辨率，使其适用于X射线晶体学研究。
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