1J06

Crystal structure of mouse acetylcholinesterase in the apo form

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-4
Synchrotron site	ESRF
Beamline	ID14-4
Temperature [K]	100
Detector technology	CCD
Detector	ADSC QUANTUM 4
Wavelength(s)	0.946
Spacegroup name	P 21 21 21
Unit cell lengths	79.196, 111.974, 226.834
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.350
Rwork	0.209
R-free	0.23200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1maa
RMSD bond length	0.013
RMSD bond angle	24.200 *
Data reduction software	DENZO
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000 *
High resolution limit [Å]	2.350
Rmerge	0.058 *	0.370 *
Total number of observations	903557 *
Number of reflections	83956
<I/σ(I)>	9.5
Completeness [%]	99.2	99.6 *
Redundancy	5.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		4 *	PEG 600, HEPES OR SODIUM ACETATE, pH 6.5-8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10-12 (mg/ml)
2	1	reservoir	PEG600	25-32 (%(v/v))
3	1	reservoir	HEPES	20-100 (mM)	pH6.5-8.0