Boulot G, Bentley G A, Karjalainen K, Mariuzza R A
URA 359 CNRS, Institut Pasteur, Paris, France.
J Mol Biol. 1994 Jan 14;235(2):795-7. doi: 10.1006/jmbi.1994.1037.
A secreted form of the beta-chain of a T-cell receptor specific for a hemagglutinin peptide of influenza virus in the context of the major histocompatibility complex class II I-Ed molecule has been crystallized in a form suitable for X-ray diffraction analysis. The crystals are tetragonal, space group P4(1)2(1)2 (or P4(3)2(1)2), with cell dimensions a = b = 71.4 A, c = 312.9 A, and diffract to beyond 3.5 A resolution. The beta-chain appears to behave as a stable homodimer in solution.
在主要组织相容性复合体II类I-Ed分子的背景下，针对流感病毒血凝素肽具有特异性的T细胞受体β链的一种分泌形式已结晶为适合X射线衍射分析的形式。晶体为四方晶系，空间群P4(1)2(1)2（或P4(3)2(1)2），晶胞参数a = b = 71.4 Å，c = 312.9 Å，衍射分辨率超过3.5 Å。β链在溶液中似乎表现为稳定的同二聚体。
