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 (%)