1GQR

ACETYLCHOLINESTERASE (E.C. 3.1.1.7) COMPLEXED WITH RIVASTIGMINE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X12C
Synchrotron site	NSLS
Beamline	X12C
Temperature [K]	100
Collection date	1997-07-15
Spacegroup name	P 31 2 1
Unit cell lengths	112.052, 112.052, 136.770
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	29.200 * - 2.200
R-factor	0.199
Rwork	0.199
R-free	0.23600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ACE
RMSD bond length	0.006
RMSD bond angle	23.700 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.280
High resolution limit [Å]	2.200	2.200
Rmerge	0.066	0.322
Total number of observations	242981 *
Number of reflections	46214 *
<I/σ(I)>	17.7	1.4
Completeness [%]	99.7	97.1
Redundancy	4.8	2.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	5.8	4 *	pH 5.80

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG200	34-38 (%(v/v))
2	1	reservoir	MES	0.1 (M)	pH5.8
3	1	drop	protein	11 (mg/ml)