1FV1

STRUCTURAL BASIS FOR THE BINDING OF AN IMMUNODOMINANT PEPTIDE FROM MYELIN BASIC PROTEIN IN DIFFERENT REGISTERS BY TWO HLA-DR2 ALLELES

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X12B
Synchrotron site	NSLS
Beamline	X12B
Temperature [K]	100
Detector technology	CCD
Collection date	1999-11-07
Detector	ADSC QUANTUM 4
Spacegroup name	P 1 21 1
Unit cell lengths	63.189, 114.892, 63.175
Unit cell angles	90.00, 90.90, 90.00

Refinement procedure

Resolution	100.000 - 1.900
R-factor	0.233
Rwork	0.233
R-free	0.26700
RMSD bond length	0.006
RMSD bond angle	1.500
Data reduction software	DENZO
Data scaling software	CCP4 ((TRUNCATE))
Phasing software	AMoRE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	100.000	1.990
High resolution limit [Å]	1.900	1.900
Rmerge	0.081	0.349
Total number of observations	181399 *
Number of reflections	63997 *
<I/σ(I)>	0.081
Completeness [%]	90.8 *	75.6 *
Redundancy	2.8	2.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6.5	298	2/3 dilution of 30% PEG 8000, 0.1M sodium cacodylate, pH6.5, 0.2M ammonium sulfate, EVAPORATION, temperature 298.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5 (mg/ml)
2	1	reservoir	PEG8000	30 (%(w/v))
3	1	reservoir	sodium cacodylate	0.1 (M)
4	1	reservoir	ammonium sulfate	0.2 (M)