1P7Q

Crystal Structure of HLA-A2 Bound to LIR-1, a Host and Viral MHC Receptor

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.3
Synchrotron site	ALS
Beamline	5.0.3
Temperature [K]	100
Detector technology	CCD
Collection date	2001-10-28
Detector	ADSC QUANTUM 4
Wavelength(s)	0.992
Spacegroup name	P 31 2 1
Unit cell lengths	113.740, 113.740, 89.460
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	50.000 * - 3.400
R-factor	0.218
Rwork	0.218
R-free	0.31000 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	PDB entries 1G0X and 1AKJ
RMSD bond length	0.021 *
RMSD bond angle	1.850 *
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	3.610
High resolution limit [Å]	3.400	3.400
Rmerge	0.180	0.505
Total number of observations	61195 *
Number of reflections	9493	928 *
<I/σ(I)>	11.7	3.8
Completeness [%]	99.9	100
Redundancy	6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5	298	PEG 4000, Sodium Acetate, Tris, L-Cysteine, Triton X-100, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	14.5 (mg/ml)
2	1	drop	sodium acetate	0.2 (M)
3	1	drop	Tris	0.1 (M)	pH8.5
4	1	drop	PEG4000	30 (%(w/v))
5	1	reservoir	sodium acetate	0.2 (M)
6	1	reservoir	Tris	0.1 (M)	pH8.5
7	1	reservoir	PEG4000	30 (%(w/v))
8	1	reservoir	L-cysteine	20 (mM)
9	1	reservoir	TritonX-100	1.8 (mM)