TY - JOUR
T1 - Crystallization of murine major histocompatibility complex class I H-2Kb with single peptides
AU - Stura, Enrico A.
AU - Matsumura, Masazumi
AU - Fremont, Daved H.
AU - Saito, Yutaka
AU - Peterson, Per A.
AU - Wilson, Lan A.
PY - 1992/12/5
Y1 - 1992/12/5
N2 - X-ray quality crystals of a soluble murine class I H-2Kb molecule complexed with three different peptide antigens were grown in several forms by streak seeding and macroseeding methods. Co-crystals with VSV-8 (RGYVYGQL), OVA-8 (SIINFEKL) and SEV-9 (FAPGNYPAL) peptides were grown either from NaH2PO4 K2HPO4 or from polyethylene glycol 4000 within the pH range 5·0 to 7·5, with the use of 4-methyl-2-pentane diol (MPD) as an additive. The VSV-8 crystals grew in space groups P1, with cell dimensions a =63·1 A ̊, b = 69·1 A ̊, c = 72·0 A ̊, α = 89·9 °, β = 77·1 °, γ = 123·3 ° and P21212, with a = 138.1 A ̊, b = 88·6 A ̊, c = 45·7 A ̊, and diffract to 2·9 and 2·3 Å, respectively. Crystals of the SEV-9 complex grew from similar crystallization conditions to those of the orthorhombic VSV-8 complex with similar cell parameters and diffract to at least 2·5 Å resolution. Crystals of the OVA-8 complex were obtained from either phosphate (space group C2, a = 118·7 A ̊, b = 61·6 A ̊, c = 85·3 A ̊, β = 108·4 °) or polyethylene glycol (space group P1, a = 64·5 A ̊, b = 71·0 A ̊, c = 66·3 A ̊, α = 89·7 °, β = 95·7 °, γ = 123·3 °) and diffract to 3 Å resolution. The crystallization procedures used here significantly increased the rate and production of X-ray quality crystals.
AB - X-ray quality crystals of a soluble murine class I H-2Kb molecule complexed with three different peptide antigens were grown in several forms by streak seeding and macroseeding methods. Co-crystals with VSV-8 (RGYVYGQL), OVA-8 (SIINFEKL) and SEV-9 (FAPGNYPAL) peptides were grown either from NaH2PO4 K2HPO4 or from polyethylene glycol 4000 within the pH range 5·0 to 7·5, with the use of 4-methyl-2-pentane diol (MPD) as an additive. The VSV-8 crystals grew in space groups P1, with cell dimensions a =63·1 A ̊, b = 69·1 A ̊, c = 72·0 A ̊, α = 89·9 °, β = 77·1 °, γ = 123·3 ° and P21212, with a = 138.1 A ̊, b = 88·6 A ̊, c = 45·7 A ̊, and diffract to 2·9 and 2·3 Å, respectively. Crystals of the SEV-9 complex grew from similar crystallization conditions to those of the orthorhombic VSV-8 complex with similar cell parameters and diffract to at least 2·5 Å resolution. Crystals of the OVA-8 complex were obtained from either phosphate (space group C2, a = 118·7 A ̊, b = 61·6 A ̊, c = 85·3 A ̊, β = 108·4 °) or polyethylene glycol (space group P1, a = 64·5 A ̊, b = 71·0 A ̊, c = 66·3 A ̊, α = 89·7 °, β = 95·7 °, γ = 123·3 °) and diffract to 3 Å resolution. The crystallization procedures used here significantly increased the rate and production of X-ray quality crystals.
KW - H-2K
KW - MHC class I
KW - X-ray crystallography
KW - additives
KW - peptide complex
KW - protein crystallization
UR - http://www.scopus.com/inward/record.url?scp=0027096461&partnerID=8YFLogxK
U2 - 10.1016/0022-2836(92)90881-J
DO - 10.1016/0022-2836(92)90881-J
M3 - Article
C2 - 1469730
AN - SCOPUS:0027096461
SN - 0022-2836
VL - 228
SP - 975
EP - 982
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 3
ER -