title: Crystallization and preliminary X-ray diffraction analysis of the beta-chain of a T-cell antigen receptor.
abstract: 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.
authors.affiliation: URA 359 CNRS, Institut Pasteur, Paris, France.
authors.forename: G
authors.initials: G
authors.lastname: Boulot
authors.forename: G A
authors.initials: GA
authors.lastname: Bentley
authors.forename: K
authors.initials: K
authors.lastname: Karjalainen
authors.forename: R A
authors.initials: RA
authors.lastname: Mariuzza
mesh_terms: D000595:Amino Acid Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D011948:Receptors, Antigen, T-Cell / Q000737:chemistry*
chemical_list: D011948:Receptors, Antigen, T-Cell