1H23

Structure of acetylcholinesterase (E.C. 3.1.1.7) complexed with (S,S)-(-)-bis(12)-hupyridone at 2.15A resolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RUH3R
Temperature [K]	120
Detector technology	IMAGE PLATE
Collection date	2000-09-05
Detector	RIGAKU IMAGE PLATE
Spacegroup name	P 31 2 1
Unit cell lengths	111.794, 111.794, 137.775
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	29.300 - 2.150
R-factor	0.1893
Rwork	0.189
R-free	0.21500 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2ace
RMSD bond length	0.020
RMSD bond angle	1.940 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	29.300	2.230
High resolution limit [Å]	2.150	2.150
Rmerge	0.066	0.396
Total number of observations	536295 *
Number of reflections	54392 *
<I/σ(I)>	13.5
Completeness [%]	99.7	99.8
Redundancy	0.38	9.79

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	5.8	4 *	PROTEIN WAS CRYSTALLISED FROM 28-30% V/V PEG 200 0.5M MES PH 5.8 AT 4 DEG. CELSIUS; THEN SOAKED IN IN MOTHER LIQUOR (40% V/V PEG 200 IN 0.1 M MES BUFFER, PH 5.8) CONTAINING 10MM (S,S)-(-)-BIS(12)-HUPYRIDONE DIHYDROCHLORIDE FOR 2 DAYS

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	PEG200	40 (%(v/v))
2	1	drop	MES	0.5 (M)	pH5.8
3	1	reservoir	PEG200	28-30 (%(v/v))
4	1	reservoir	MES	0.5 (M)	pH5.8