1MUJ

Crystal structure of murine class II MHC I-Ab in complex with a human CLIP peptide

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL11-1
Synchrotron site	SSRL
Beamline	BL11-1
Temperature [K]	95
Detector technology	IMAGE PLATE
Collection date	2001-02-17
Detector	MAR scanner 300 mm plate
Spacegroup name	C 1 2 1
Unit cell lengths	63.647, 88.065, 83.740
Unit cell angles	90.00, 92.48, 90.00

Refinement procedure

Resolution	33.060 - 2.150
R-factor	0.22
Rwork	0.220
R-free	0.25000 *
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	26.400 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	33.060	2.230
High resolution limit [Å]	2.150	2.150
Rmerge	0.038 *	0.540 *
Number of reflections	24657
<I/σ(I)>	24.1	1.65
Completeness [%]	98.0	97
Redundancy	1.87	1.83

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	22 *	PEG3000, Sodium Chloride, Tris, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295.5K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	Tris	100 (mM)	pH7.5
2	1	reservoir		200 (mM)
3	1	reservoir	PEG3000	22.5 (%)
4	1	reservoir	MPD	5 (%(v/v))
5	1	drop	protein	5-10 (mg/ml)