1HCI

CRYSTAL STRUCTURE OF THE ROD DOMAIN OF ALPHA-ACTININ

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-2
Synchrotron site	ESRF
Beamline	ID14-2
Temperature [K]	100
Detector technology	CCD
Collection date	2001-04-02
Detector	ADSC CCD
Spacegroup name	P 31
Unit cell lengths	103.280, 103.280, 218.640
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	82.780 - 2.800
R-factor	0.27
Rwork	0.270
R-free	0.29500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1quu
RMSD bond length	0.008
RMSD bond angle	18.900 *
Data reduction software	XDS
Data scaling software	XDS
Phasing software	CNS
Refinement software	CNS (0.9)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	82.780	2.900
High resolution limit [Å]	2.800	2.800
Rmerge	0.082	0.261
Total number of observations	155820 *
Number of reflections	63392
<I/σ(I)>	7.6	2.28
Completeness [%]	98.7	99
Redundancy	2.45	1.78

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8.5	20 *	0.9 M (NH4)2SO4, 0.1 M TRISHCL PH 8.5

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	7-10 (mg/ml)
2	1	drop	Tris-HCl	20 (mM)
3	1	drop	dithiothreitol	1 (mM)
4	1	reservoir	ammonium sulfate	0.9 (M)
5	1	reservoir	Tris-HCl	0.1 (M)