3PN7

Visualizing new hinges and a potential major source of compliance in the lever arm of myosin

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X29A
Synchrotron site	NSLS
Beamline	X29A
Temperature [K]	100
Detector technology	CCD
Collection date	2009-11-03
Detector	ADSC QUANTUM 315r
Wavelength(s)	1.075
Spacegroup name	P 1
Unit cell lengths	50.737, 68.779, 79.305
Unit cell angles	77.41, 85.94, 73.61

Refinement procedure

Resolution	48.672 - 2.250
R-factor	0.1913
Rwork	0.191
R-free	0.24140
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1wdc
RMSD bond length	0.008
RMSD bond angle	1.099
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	PHENIX ((phenix.refine: 2009_12_14_1757))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.330
High resolution limit [Å]	2.240	2.240
Rmerge	0.074
Number of reflections	46183
<I/σ(I)>	16.9
Completeness [%]	96.2	82
Redundancy	3.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	7	277	1.1-1.6 mg/ml protein in 5mM HEPES buffer, 20mM NaCl, 1.5mM MgCl2, 0.5-1mM CaCl2, 0.1mM EGTA, 0.5mM DTT, 2mM NaN3, 0.5 ug/ml leupeptin, 0.7 ug/ml pepstatin-A and 7.5% (w/v) of polyethylene glycol 3350 (PEG 3350) or polyethylene glycol monomethyl ether 2000 (MME PEG 2K). The reservoir solution: 10 mM HEPES, 40mM NaCl, 3 mM MgCl2, 2 mM NaN3 and 15% PEG 3350 or MME, PEG 2K, pH 7.0, VAPOR DIFFUSION, temperature 277K