Complex assembly, crystallization and preliminary X-ray crystallographic studies of the swine major histocompatibility complex molecule SLA-1*1502

A crystal of a swine MHC class I molecule diffracted to 2.2 Å resolution and belonged to space group P2₁2₁2₁, with unit-cell parameters a = 66.1, b = 74.1, c = 98.6 Å; it contained one molecule in the asymmetric unit. The Matthews coefficient and the solvent content were calculated to be 2.74 ų Da⁻¹ and 55.17%, respectively. In order to illustrate the structure of the swine MHC class I (SLA-I) molecule and to evaluate the cytotoxic T lymphocyte (CTL) response against porcine reproductive and respiratory syndrome virus (PRRSV), the ternary complex of the SLA-I molecule termed SLA-1*1502 with β₂-microglobulin and the CTL epitope TMPPGFELY (PRRSV-NSP9_TY9) derived from PRRSV nonstructural protein 9 (residues 198–206) was assembled and crystallized. The crystal diffracted X-rays to 2.2 Å resolution and belonged to space group P2₁2₁2₁, with unit-cell parameters a = 66.1, b = 74.1, c = 98.6 Å; it contained one molecule in the asymmetric unit. The Matthews coefficient and the solvent content were calculated to be 2.74 ų Da⁻¹ and 55.17%, respectively. The results will be helpful in obtaining insight into the structural basis of the presentation of viral epitopes by SLA-I