1OCE

ACETYLCHOLINESTERASE (E.C. 3.1.1.7) COMPLEXED WITH MF268

Experimental procedure

Source type	SYNCHROTRON
Source details	ELETTRA BEAMLINE 5.2R
Synchrotron site	ELETTRA
Beamline	5.2R
Temperature [K]	120
Detector technology	IMAGE PLATE AREA DETECTOR
Collection date	1997-06
Detector	MARRESEARCH
Spacegroup name	P 31 2 1
Unit cell lengths	111.496, 111.496, 137.390
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	8.000 - 2.700
R-factor	0.208
Rwork	0.208
R-free	0.29100
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2ace
RMSD bond length	0.008
RMSD bond angle	27.100 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	X-PLOR

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.800
High resolution limit [Å]	2.700	2.700
Rmerge	0.140 *	0.648 *
Total number of observations	248837 *
Number of reflections	24049	1886 *
<I/σ(I)>	6.7	1.7
Completeness [%]	87.2	69.7
Redundancy	2.3	1.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6		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)