Crystallization and preliminary crystallographic studies of the single-chain variable fragment of antibody chA21 in complex with an N-terminal fragment of ErbB2.
ErbB2 is a transmembrane tyrosine kinase, the overexpression of which causes abnormality and disorder in cell signalling and leads to cell transformation. Previously, an anti-ErbB2 single-chain chimeric antibody chA21 that specifically inhibits the growth of ErbB2-overexpressing cancer cells in vitro and in vivo was developed. Here, an antibody-antigen complex consisting of the single-chain variable fragment (scFv) of chA21 and an N-terminal fragment (residues 1-192, named EP I) of the ErbB2 extracellular domain was crystallized using the sitting-drop vapour-diffusion method. An X-ray diffraction data set was collected to 2.45 A resolution from a single flash-cooled crystal; the crystal belonged to space group P2(1)2(1)2(1).
Liu
Yang
Y
School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, People's Republic of China.
Zhou
Huihao
H
Zhu
Juanjuan
J
Gao
Yongxiang
Y
Niu
Liwen
L
Liu
Jing
J
Teng
Maikun
M
D000818:Animals; D000906:Antibodies / Q000737:chemistry*; D016466:CHO Cells; D006224:Cricetinae; D003412:Cricetulus; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D007135:Immunoglobulin Variable Region / Q000737:chemistry*; D018719:Erb-b2 Receptor Tyrosine Kinases / Q000737:chemistry*
D000906:Antibodies; D007135:Immunoglobulin Variable Region; D018719:Erb-b2 Receptor Tyrosine Kinases