3WTO

Crystal Structure of Lymnaea stagnalis Acetylcholine-Binding Protein Q55R Mutant Complexed with Desnitro-imidacloprid

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL26B2
Synchrotron site	SPring-8
Beamline	BL26B2
Temperature [K]	100
Detector technology	CCD
Collection date	2008-07-03
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.9
Spacegroup name	P 21 21 21
Unit cell lengths	73.056, 120.742, 139.346
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.780 - 2.250
R-factor	0.215
Rwork	0.215
R-free	0.26200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2zju
RMSD bond length	0.007
RMSD bond angle	1.400
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	PHASER
Refinement software	CNS (1.2)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.330
High resolution limit [Å]	2.250	2.250
Rmerge	0.076	0.449
Number of reflections	58935
<I/σ(I)>	38.2	4.9
Completeness [%]	99.8	99.7
Redundancy	7.3	7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	8.5	293	24-27 % PEG4000, 0.1-0.3M LiSO4, 0.1M Tris-HCl, pH 8.5, 0.5mM Desnitro-imidacloprid, VAPOR DIFFUSION, temperature 293K