1HSA
THE THREE-DIMENSIONAL STRUCTURE OF HLA-B27 AT 2.1 ANGSTROMS RESOLUTION SUGGESTS A GENERAL MECHANISM FOR TIGHT PEPTIDE BINDING TO MHC
Experimental procedure
Spacegroup name | P 1 |
Unit cell lengths | 45.100, 69.800, 81.100 |
Unit cell angles | 80.30, 88.60, 89.90 |
Refinement procedure
Resolution | 5.500 * - 2.100 |
R-factor | 0.203 |
Rwork | 0.203 |
R-free | 0.26700 * |
RMSD bond length | 0.016 |
RMSD bond angle | 2.800 |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 10.000 * |
High resolution limit [Å] | 2.100 * |
Rmerge | 0.077 * |
Completeness [%] | 92.0 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8.5 * | THE FRAGMENT CRYSTALLIZED WAS THE EXTRACELLULAR PORTION OF THE PROTEIN CLEAVED FROM DETERGENT MICELLES WITH PAPAIN |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | polyethylen glycol 3350 | 24 (%) | |
2 | 1 | reservoir | sodium acetate | 250 (mM) | |
3 | 1 | reservoir | Tris | 100 (mM) | |
4 | 1 | reservoir | MES | 25 (mM) | |
5 | 1 | reservoir | sodium azide | 0.1 (%) |