Complex assembly, crystallization and preliminary X-ray crystallographic analysis of the bovine CD8αα–BoLA-2*02201 complex

The crystallization and preliminary X-ray diffraction analysis of a complex between bovine CD8αα and the bovine MHC class I molecule (BoLA-I, BoLA-2*02201) at 1.7 Å resolution revealed that the crystal belonged to space group P2₁, with unit-cell parameters a = 53.9, b = 103.8, c = 61.8 Å, α = γ = 90, β = 96°, and contained one complex in the asymmetric unit. The Matthews coefficient and solvent content were calculated as 2.41 ų Da⁻¹ and 48.9%, respectively.

Crystallization and preliminary crystallographic studies of the complement 1qA globular domain from zebrafish, Dare-C1qAgD

The crystal structure of zebrafish (D. rerio) complement 1qA globular domain (Dare-C1qAgD) was determined from X-ray diffraction data collected to 2.05 Å resolution. The crystal belonged to the orthorhombic space group P2₁2₁2₁, with unit-cell parameters a = 50.347, b = 85.059, c = 95.560 Å.

Crystallization and preliminary X-ray diffraction analysis of a single variable domain of the immunoglobulin superfamily in amphioxus, Amphi-IgSF-V

X-ray diffraction data for Amphi-IgSF-V (a single variable domain of the immunoglobulin superfamily from amphioxus) were collected to 1.95 Å resolution. The crystal belonged to space group P3₂21, with unit-cell parameters a = b = 53.9, c = 135.5 Å, and contained two molecules in the asymmetric unit. The Matthews coefficient and solvent content were calculated to be 2.58 Å³ Da^-1 and 52.38%, respectively.

Complex assembly, crystallization and preliminary X-ray crystallographic analysis of the chicken CD8αα–BF2*0401 complex

A crystal of the chicken MHC class I molecule BF2*0401 in complex with chicken CD8αα (CD8αα–BF2*0401) diffracted to 2.8 Å resolution and belonged to space group P2₁, with unit-cell parameters a = 90.6, b = 90.8, c = 94.9 Å, β = 98°.