1N5R

Crystal structure of the mouse acetylcholinesterase-propidium complex

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-2
Synchrotron site	ESRF
Beamline	ID14-2
Temperature [K]	100
Wavelength(s)	0.933
Spacegroup name	P 21 21 21
Unit cell lengths	79.552, 111.665, 226.834
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 * - 2.250
R-factor	0.204
Rwork	0.204
R-free	0.22600 *
Structure solution method	FOURIER SYNTHESIS
RMSD bond length	0.011 *
RMSD bond angle	1.800 *
Data reduction software	DENZO
Data scaling software	SCALA
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000 *
High resolution limit [Å]	2.250
Rmerge	0.041 *	0.386 *
Total number of observations	549001 *
Number of reflections	95908
<I/σ(I)>	13.5
Completeness [%]	99.5	98.9 *
Redundancy	3.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		4 *	PEG 600, 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
4	1	reservoir	PI	2-5 (mM)