1GQS

ACETYLCHOLINESTERASE (E.C. 3.1.1.7) COMPLEXED WITH NAP

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1999-08-15
Spacegroup name	P 31 2 1
Unit cell lengths	111.040, 111.040, 137.227
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	29.200 - 3.000
R-factor	0.212
Rwork	0.212
R-free	0.26200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ACE
RMSD bond length	0.008
RMSD bond angle	23.000 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	29.200	3.110
High resolution limit [Å]	3.000	3.000
Rmerge	0.160	0.529 *
Total number of observations	243327 *
Number of reflections	20097 *
<I/σ(I)>	5	1.4
Completeness [%]	99.4	98.4 *
Redundancy	5.3

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)