3BAT

Crystal structure of the N-terminal region of the scallop myosin rod, monoclinic (P21) form

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X26C
Synchrotron site	NSLS
Beamline	X26C
Temperature [K]	100
Detector technology	CCD
Detector	ADSC QUANTUM 4
Wavelength(s)	0.97910
Spacegroup name	P 1 21 1
Unit cell lengths	65.782, 40.217, 77.404
Unit cell angles	90.00, 111.54, 90.00

Refinement procedure

Resolution	30.000 - 2.300
R-factor	0.253
Rwork	0.253
R-free	0.29900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1nkn
RMSD bond length	0.007
RMSD bond angle	0.864
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]	30.000	30.000	2.020
High resolution limit [Å]	1.950	4.200	1.950
Rmerge	0.052	0.037	0.290
Number of reflections	27340
<I/σ(I)>	13.8
Completeness [%]	98.5	93.4	95.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.2	277	2 microliters of protein solution (4 mg/ml protein in 30 mM MOPS buffer pH 7.2, 40 mM NaCl, 2 mM NaN3) mixed with 2 microliters of (25% PEG 3350, 50 mM NH4I) and equilibrated against 1 ml of (17.5% PEG 3350, 35 mM NH4I, 28 mM NaCl, 2 mM NaN3, 20 mM MOPS pH 6.2). Harvested crystals were cryoprotected in 25.5% PEG 3350 and 15% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 277K