1Q84

Crystal structure of the mouse acetylcholinesterase-TZ2PA6 anti 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
Detector technology	CCD
Collection date	2002-12-05
Detector	ADSC QUANTUM 4
Wavelength(s)	0.933
Spacegroup name	P 21 21 21
Unit cell lengths	79.272, 111.765, 227.171
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	25.000 * - 2.450
R-factor	0.18487
Rwork	0.184
R-free	0.21400 *
Structure solution method	FOURIER SYNTHESIS
Starting model (for MR)	1j06
RMSD bond length	0.015
RMSD bond angle	1.500
Data reduction software	DENZO
Data scaling software	CCP4 ((SCALA))
Phasing software	CNS
Refinement software	REFMAC (5.1.24)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000 *
High resolution limit [Å]	2.450
Rmerge	0.057 *	0.435 *
Total number of observations	549476 *
Number of reflections	74834
<I/σ(I)>	9.3
Completeness [%]	99.8	99.7 *
Redundancy	3.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.75	4 *	25-32% PEG 600, 20-100 mM Hepes, pH 6.75, VAPOR DIFFUSION, HANGING DROP, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG600	25-32 (%(v/v))
2	1	reservoir	HEPES	20-100 (mM)	pH6.0-7.5