1JPF

Crystal Structure Of The LCMV Peptidic Epitope Gp276 In Complex With The Murine Class I Mhc Molecule H-2Db

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM1A
Synchrotron site	ESRF
Beamline	BM1A
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1999-02-28
Detector	MARRESEARCH
Wavelength(s)	0.873
Spacegroup name	P 43 21 2
Unit cell lengths	56.166, 56.166, 277.954
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 - 2.180
R-factor	0.211 *
Rwork	0.211
R-free	0.26200
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.010 *
RMSD bond angle	1.490 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (0.9)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.230
High resolution limit [Å]	2.180	2.180
Rmerge	0.082 *	0.293 *
Number of reflections	24648	1569 *
Completeness [%]	99.8	98.3
Redundancy	8.6 *	6.9 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.4	4 *	Ammonium phosphate, PEG8000, Tris-HCl, pH 6.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10.6 (mg/ml)
2	1	reservoir	ammonium phosphate	0.2 (M)
3	1	reservoir	PEG8000	25 (%)
4	1	reservoir	Tris-HCl	0.1 (M)
5	1	reservoir	sodium azide	0.02 (%(w/v))