2SEB

X-RAY CRYSTAL STRUCTURE OF HLA-DR4 COMPLEXED WITH A PEPTIDE FROM HUMAN COLLAGEN II

Experimental procedure

Source type	SYNCHROTRON
Source details	CHESS BEAMLINE F1
Synchrotron site	CHESS
Beamline	F1
Temperature [K]	173
Detector technology	CCD
Collection date	1996-10
Spacegroup name	P 21 21 21
Unit cell lengths	78.530, 100.280, 100.870
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	12.000 - 2.500
R-factor	0.229
Rwork	0.229
R-free	0.28000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1seb
RMSD bond length	0.007
RMSD bond angle	1.500
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]	30.000	2.570
High resolution limit [Å]	2.500	2.500
Rmerge	0.081	0.218
Total number of observations	178959 *
Number of reflections	27635
<I/σ(I)>	10	3.9
Completeness [%]	87.7	83.7
Redundancy	6	2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	unknown *	4.6	25 *	0.1 M NA ACETATE PH 4.6 9 - 14% PEG 4000 0.2 M AMMONIUM ACETATE

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	protein	8 (mg/ml)
2	1	2	sodium acetate	0.1 (M)
3	1	2	PEG4000	9-14 (%)
4	1	2	ammonium acetate	0.2 (M)