3BAS

Crystal structure of the N-terminal region of the scallop myosin rod, monoclinic (C2) form

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	CHESS BEAMLINE A1
Synchrotron site	CHESS
Beamline	A1
Temperature [K]	100
Detector technology	CCD
Detector	ADSC QUANTUM 210
Wavelength(s)	0.9764
Spacegroup name	C 1 2 1
Unit cell lengths	123.335, 44.912, 39.878
Unit cell angles	90.00, 95.18, 90.00

Refinement procedure

Resolution	20.000 - 2.300
R-factor	0.246
Rwork	0.246
R-free	0.28700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1nkn
RMSD bond length	0.006
RMSD bond angle	0.880
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.380
High resolution limit [Å]	2.300	4.950	2.300
Rmerge	0.082	0.044	0.245
Number of reflections	8283
<I/σ(I)>	9.9
Completeness [%]	84.9	98.8	53.6
Redundancy	3.3	3.5	2.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.2	277	1.5 microliter of protein solution (4 mg/ml protein in 30 mM MOPS buffer pH 7.2, 40 mM NaCl, 2 mM NaN3) mixed with 3 microliters of (16.6% PEG 3350, 4.6% MPD, 13 mM NaCl, 2 mM NaN3, 10 mM MOPS pH 7.2) and equilibrated against (15% PEG 3350, 4.2% MPD, 18 mM MOPS, 24 mM NaCl), VAPOR DIFFUSION, HANGING DROP, temperature 277K