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Production and crystallization of MHC class I B allele single peptide complexes
Author(s) -
Reid Scott W.,
Smith Kathrine J.,
Jakobsen Bent K.,
O'Callaghan Chris A.,
Reyburn Hugh,
Harlos Karl,
Stuart David I.,
McMichael Andrew J.,
Bell John I.,
Jones E.Yvonne
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00226-8
Subject(s) - crystallization , allele , major histocompatibility complex , human leukocyte antigen , biology , chemistry , mhc class i , genetics , microbiology and biotechnology , crystallography , antigen , gene , organic chemistry
Major histocompatibility complex class I B alleles, HLA B8, B53 and B3501 have been cloned, expressed, refolded and crystallized in specific complexes with a number of different 8‐mer and 9‐mer peptides. For some of these crystallization was initiated by cross‐seeding between different B allele complexes. All crystallize in the space group P2 1 2 1 2 1 , with similar unit cell dimensions of approximately , contain one complex per asymmetric unit and diffract to approximately 2.0 Å resolution.