1C5D

THE CRYSTAL STRUCTURE OF THE FAB FRAGMENT OF A RAT MONOCLONAL ANTIBODY AGAINST THE MAIN IMMUNOGENIC REGION OF THE HUMAN MUSCLE ACETYLCHOLINE RECEPTOR

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ELETTRA BEAMLINE 5.2R
Synchrotron site	ELETTRA
Beamline	5.2R
Temperature [K]	100
Collection date	1996-07-01
Spacegroup name	C 2 2 21
Unit cell lengths	79.710, 110.080, 199.520
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.400
R-factor	0.196
Rwork	0.196
R-free	0.30400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2cgr
RMSD bond length	0.010
RMSD bond angle	30.800 *
Data reduction software	AUTOMAR
Data scaling software	XDS
Phasing software	X-PLOR
Refinement software	X-PLOR (3.8)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.500
High resolution limit [Å]	2.400	2.400
Rmerge	0.087	0.232
Total number of observations	118352 *
Number of reflections	26381
<I/σ(I)>	25.45	9.12
Completeness [%]	76.1	51.9
Redundancy	4.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	unknown *	7.5	16 *	12 MG/ML FAB192, 18% W/V PEG6000, 150 MM NACL, 100 MM BIS-TRIS/HCL, PH 7.5, 2 MM EDTA, AT 16 DEG. C, temperature 289K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	12 (mg/ml)
2	1	reservoir	PEG6000	18 (%(w/v))
3	1	reservoir		150 (mM)
4	1	reservoir	bis-Tris-HCl	100 (mM)
5	1	reservoir	EDTA	2 (mM)