4DAJ

Structure of the M3 Muscarinic Acetylcholine Receptor

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-D
Synchrotron site	APS
Beamline	23-ID-D
Temperature [K]	78
Detector technology	CCD
Collection date	2011-08-14
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	1.033
Spacegroup name	P 1
Unit cell lengths	54.770, 61.310, 176.910
Unit cell angles	85.87, 89.90, 84.90

Refinement procedure

Resolution	39.900 - 3.400
R-factor	0.254
Rwork	0.251
R-free	0.30300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	M2 muscarinic acetylcholine receptor (3UON)
RMSD bond length	0.011
RMSD bond angle	0.862
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	PHENIX ((phenix.refine: 1.7_650))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	3.500
High resolution limit [Å]	3.400	3.400
Rmerge	0.226	0.527
Number of reflections	28385
<I/σ(I)>	4.5	1.7
Completeness [%]	90.6	85.9
Redundancy	3.7	2.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1		7.5	293	27-38% PEG 300, 100 mM HEPES pH 7.5, 1% (w/w) 1,2,3-heptanetriol, and 100 mM ammonium phosphate. Protein was reconstituted in cubic phase using a 10:1 monolein:cholesterol mix by weight, Lipidic cubic phase, temperature 293K
1		7.5	293	27-38% PEG 300, 100 mM HEPES pH 7.5, 1% (w/w) 1,2,3-heptanetriol, and 100 mM ammonium phosphate. Protein was reconstituted in cubic phase using a 10:1 monolein:cholesterol mix by weight, Lipidic cubic phase, temperature 293K