1OF2

Crystal structure of HLA-B*2709 complexed with the vasoactive intestinal peptide type 1 receptor (VIPR) peptide (residues 400-408)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X13
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X13
Temperature [K]	100
Detector technology	CCD
Collection date	2002-11-15
Detector	MARRESEARCH
Spacegroup name	P 1 21 1
Unit cell lengths	51.158, 81.635, 65.310
Unit cell angles	90.00, 107.47, 90.00

Refinement procedure

Resolution	29.100 * - 2.200
R-factor	0.191
Rwork	0.188
R-free	0.24400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1k5n
RMSD bond length	0.010
RMSD bond angle	1.300 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	REFMAC (5.1.19)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	29.100	2.280
High resolution limit [Å]	2.200	2.200
Rmerge	0.123 *	0.346 *
Number of reflections	25005	2495 *
<I/σ(I)>	9.7	4.1
Completeness [%]	95.8 *	96.8 *
Redundancy	3.1	3.0 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5 *	291	TRIS PH 8.5, 19% PEG 8000 HANGING DROP, TEMPERATURE 291K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	Tris-HCl	0.1 (M)	pH8.5
2	1	reservoir	PEG8000	19 (%)
3	1	drop	protein	16 (mg/ml)
4	1	drop	Tris-HCl	10 (mM)	pH7.5
5	1	drop		150 (mM)