1UX4

Crystal structures of a Formin Homology-2 domain reveal a tethered-dimer architecture

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 8-BM
Synchrotron site	APS
Beamline	8-BM
Temperature [K]	100
Spacegroup name	C 1 2 1
Unit cell lengths	98.100, 172.200, 120.600
Unit cell angles	90.00, 112.30, 90.00

Refinement procedure

Resolution	30.000 * - 3.300
R-factor	0.234
Rwork	0.234
R-free	0.28800 *
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	1.370 *
Data scaling software	SCALEPACK
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000
High resolution limit [Å]	3.300
Rmerge	0.058	0.143 *
Total number of observations	50090 *
Number of reflections	22747
<I/σ(I)>	12.5
Completeness [%]	82.0	61 *
Redundancy	2.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	20 *	HANGING DROP AGAINST 0.8M SODIUM POTASSIUM PHOSPHATE, 30% GLYCEROL, HEPES PH7.5, pH 7.50

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	8 (mg/ml)
2	1	drop	PCMBS	2.5 (mM)
3	1	reservoir	sodium potassium phosphate	0.8 (M)
4	1	reservoir	HEPES	100 (mM)	pH7.5
5	1	reservoir	glycerol	30 (%)