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