1JHT

Crystal structure of HLA-A2*0201 in complex with a nonameric altered peptide ligand (ALGIGILTV) from the MART-1/Melan-A.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 14-BM-C
Synchrotron site	APS
Beamline	14-BM-C
Temperature [K]	100
Detector technology	CCD
Collection date	2000-03-26
Detector	ADSC QUANTUM 4
Wavelength(s)	1.0
Spacegroup name	P 21 21 21
Unit cell lengths	49.190, 74.470, 122.290
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.690 - 2.150
R-factor	0.21
Rwork	0.210
R-free	0.25200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1DUZ (peptide removed)
RMSD bond length	0.006
RMSD bond angle	1.300
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	CNS (0.9)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.250
High resolution limit [Å]	2.150	2.150
Rmerge	0.039	0.124
Total number of observations	190647 *
Number of reflections	25511	3085 *
<I/σ(I)>	36	8.2
Completeness [%]	99.0	96.4
Redundancy	7.4	6.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	20 *	16% PEG, 25 mM MES, 0.10% NaN3, pH 6.5, VAPOR DIFFUSION, HANGING DROP, at 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	MES	25 (mM)
3	1	reservoir	PEG6000	16 (%)
4	1	reservoir	MES	25 (mM)
5	1	reservoir		0.10 (%)