2FY5

Structures of ligand bound human choline acetyltransferase provide insight into regulation of acetylcholine synthesis

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RUH3R
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2005-11-16
Detector	MARRESEARCH
Wavelength(s)	1.5418
Spacegroup name	P 21 21 21
Unit cell lengths	55.270, 74.030, 165.830
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	17.990 - 2.600
R-factor	0.276
Rwork	0.237
R-free	0.28500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1q6x
RMSD bond length	0.007
RMSD bond angle	1.300
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	40.000	40.000	2.690
High resolution limit [Å]	2.600	5.600	2.600
Rmerge	0.133	0.076	0.530
Number of reflections	21009	2363	1836
<I/σ(I)>	6.2
Completeness [%]	95.7
Redundancy	18.4	17	16.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	277	11-13% PEG 3350, 0.1M Tris-HCl, crystal soaked in 20mM S-(2-oxopropyl)-coenzyme A, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K