1INQ

Structure of Minor Histocompatibility Antigen peptide, H13a, complexed to H2-Db

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X9B
Synchrotron site	NSLS
Beamline	X9B
Temperature [K]	100
Detector technology	CCD
Collection date	1999-11-17
Detector	MARRESEARCH
Wavelength(s)	0.9795
Spacegroup name	C 1 2 1
Unit cell lengths	92.640, 109.420, 57.560
Unit cell angles	90.00, 120.01, 90.00

Refinement procedure

Resolution	20.000 * - 2.200
R-factor	0.209 *
Rwork	0.208
R-free	0.26100 *
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.010
RMSD bond angle	1.550 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.270
High resolution limit [Å]	2.200	2.200
Rmerge	0.058	0.075
Total number of observations	109562 *
Number of reflections	25365
<I/σ(I)>	24.4
Completeness [%]	99.0	83.4
Redundancy	4.3	3.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	18 *	12% PEG 4000, 0.1 M Hepes, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 290K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	PEG4000	12 (%)
2	1	drop	HEPES	0.1 (M)	pH7.0