Purification, crystallization and preliminary X-ray diffraction analysis of the human major histocompatibility antigen HLA-B*2703 complexed with a viral peptide and with a self-peptide

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Abstract
The product of the human leukocyte antigen (HLA) gene HLA-B*2703 differs from that of the prototypical subtype HLA-B*2705 by a single amino acid at heavy-chain residue 59 that is involved in anchoring the peptide N-terminus within the A pocket of the molecule. Two B*2703-peptide complexes were crystallized using the hanging-drop vapour-diffusion method using PEG 8000 as a precipitant. The crystals belong to space group P21 (pVIPR peptide) or P212121 (pLMP2 peptide). Data sets were collected to 1.55 Å (B*2703-pVIPR) or 2.0 Å (B*2703-pLMP2) resolution using synchrotron radiation. With B*2705-pVIPR as a search model, a clear molecular-replacement solution was found for both B*2703 complexes.