1FN4

CRYSTAL STRUCTURE OF FAB198, AN EFFICIENT PROTECTOR OF ACETYLCHOLINE RECEPTOR AGAINST MYASTHENOGENIC ANTIBODIES

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ELETTRA BEAMLINE 5.2R
Synchrotron site	ELETTRA
Beamline	5.2R
Temperature [K]	100
Spacegroup name	I 41 2 2
Unit cell lengths	169.780, 169.780, 182.570
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.800
R-factor	0.198
Rwork	0.198
R-free	0.29400
RMSD bond length	0.012
RMSD bond angle	28.500 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.900
High resolution limit [Å]	2.800	2.800
Rmerge	0.046	0.217
Total number of observations	112032 *
Number of reflections	32382
Completeness [%]	98.0	98.9
Redundancy	4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8.1 *	18 *	12 MG/ML FAB198, 1.6 M AS, 0.4 M CACL2, 0.1 M PB, 0.1% PEG 10000, PH 7.5, VAPOR DIFFUSION, SITTING DROP

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	12 (mg/ml)
2	1	reservoir	ammonium sulfate	1.6 (M)
3	1	reservoir		0.4 (M)
4	1	reservoir	phosphate	0.1 (M)	pH8.1
5	1	reservoir	PEG10000	0.1 (%)