1QTI

Acetylcholinesterase (E.C.3.1.1.7)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ELETTRA BEAMLINE 5.2R
Synchrotron site	ELETTRA
Beamline	5.2R
Temperature [K]	120
Detector technology	IMAGE PLATE
Collection date	1998-05-13
Detector	MARRESEARCH
Spacegroup name	P 31 2 1
Unit cell lengths	110.824, 110.824, 136.445
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	8.000 * - 2.500
R-factor	0.192
Rwork	0.192
R-free	0.23600
RMSD bond length	0.006
RMSD bond angle	1.200
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.400
High resolution limit [Å]	2.300	2.300
Rmerge	0.071	0.210
Total number of observations	188745 *
Number of reflections	42574 *	5493 *
<I/σ(I)>	7.7
Completeness [%]	96.1	85.9
Redundancy	4.4	2.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6 *	277	Sussman, J.L., (1988) J. Mol. Biol., 203, 821. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG200	35 (%)
2	1	drop	protein	8-10 (mg/ml)
3	1	drop	PEG200	18 (%)
4	1	drop	MES	0.5 (M)