1VZJ

Structure of the tetramerization domain of acetylcholinesterase: four-fold interaction of a WWW motif with a left-handed polyproline helix

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X4A
Synchrotron site	NSLS
Beamline	X4A
Temperature [K]	100
Collection date	2001-04-15
Wavelength(s)	0.96672,0.97927,0.97895,1.5415
Spacegroup name	P 1 21 1
Unit cell lengths	53.730, 58.790, 58.800
Unit cell angles	90.00, 111.38, 90.00

Refinement procedure

Resolution	40.000 - 2.350
R-factor	0.247
Rwork	0.247
R-free	0.25900
Structure solution method	MAD
RMSD bond length	0.009
RMSD bond angle	1.202
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SOLVE/RESOLVE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	29.000	2.380
High resolution limit [Å]	2.300	2.300
Rmerge	0.054	0.349
Number of reflections	12935
<I/σ(I)>	11.1	1.47
Completeness [%]	89.4	58.5
Redundancy	2.7	1.75

Crystallization Conditions

crystal ID	method	pH	temperature	details
1		5.6		10% ISOPROPANOL, 10% PEG, 4K 0.05 M TRISODIUM CITRATE, PH 5.6