1GPK

Structure of Acetylcholinesterase Complex with (+)-Huperzine A at 2.1A Resolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-2
Synchrotron site	ESRF
Beamline	ID14-2
Temperature [K]	100
Detector technology	CCD
Collection date	2000-05-10
Detector	BRUKER-AXS
Spacegroup name	P 31 2 1
Unit cell lengths	111.421, 111.421, 137.145
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.000 - 2.100
R-factor	0.1886
Rwork	0.189
R-free	0.21400 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ea5
RMSD bond length	0.006
RMSD bond angle	1.320
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.180
High resolution limit [Å]	2.100	2.100
Rmerge	0.044	0.416 *
Total number of observations	677200 *
Number of reflections	57502 *
<I/σ(I)>	15.2	2
Completeness [%]	98.8	99.9
Redundancy	2.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	5.8	4 *	Raves, M.L., (1997) Nature Struct. Biol., 4, 57. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG200	38 (%)
2	1	reservoir	MES	0.1 (M)
3	1	drop	protein	12 (mg/ml)