1KG0

Structure of the Epstein-Barr Virus gp42 Protein Bound to the MHC class II Receptor HLA-DR1

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 5ID-B
Synchrotron site	APS
Beamline	5ID-B
Temperature [K]	101
Detector technology	CCD
Collection date	2001-02-25
Detector	MARRESEARCH
Wavelength(s)	1.000
Spacegroup name	P 63 2 2
Unit cell lengths	170.400, 170.400, 101.000
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	30.000 - 2.650
R-factor	0.221 *
Rwork	0.221
R-free	0.24700
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	1.580
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]	30.000	2.820
High resolution limit [Å]	2.650	2.650
Rmerge	0.057 *	0.426 *
Total number of observations	181993 *
Number of reflections	25186
Completeness [%]	98.4	99.1
Redundancy	7.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.6	27 *	PEG 4000, Ammonium Acetate, Sodium Chloride, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 300K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	7 (mg/ml)
2	1	reservoir	PEG4000	9 (%)
3	1	reservoir	ammonium acetate	0.1 (M)	pH4.6
4	1	reservoir		75 (mM)