1AQD

HLA-DR1 (DRA, DRB1 0101) HUMAN CLASS II HISTOCOMPATIBILITY PROTEIN (EXTRACELLULAR DOMAIN) COMPLEXED WITH ENDOGENOUS PEPTIDE

Experimental procedure

Source type	SYNCHROTRON
Source details	CHESS BEAMLINE F1
Synchrotron site	CHESS
Beamline	F1
Temperature [K]	98
Detector technology	IMAGE PLATE
Collection date	1995-02
Detector	FUJI
Spacegroup name	C 1 2 1
Unit cell lengths	134.514, 134.320, 131.232
Unit cell angles	90.00, 104.82, 90.00

Refinement procedure

Resolution	6.000 - 2.450
R-factor	0.216
Rwork	0.216
R-free	0.27900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1dlh
RMSD bond length	0.016
RMSD bond angle	26.000 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.570
High resolution limit [Å]	2.450	2.450
Rmerge	0.070 *	0.331 *
Total number of observations	157895 *
Number of reflections	73538	7700 *
<I/σ(I)>	14.9	4.4
Completeness [%]	85.0	70
Redundancy	2.1	1.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	unknown *	3.5		CRYSTALS GREW AS NEEDLES FROM 10MG/ML HLA-DR1 / PEPTIDE COMPLEX, 15% PEG 4000, 100MM GLYCINE, PH 3.5, AT ROOM TEMPERATURE, OVER ONE WEEK.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	protein	10 (mg/ml)
2	1	1	PEG4000	15 (%)
3	1	1	glycine	100 (mM)