1HH4

Rac1-RhoGDI complex involved in NADPH oxidase activation

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-4
Synchrotron site	ESRF
Beamline	ID14-4
Temperature [K]	100
Spacegroup name	P 21 21 2
Unit cell lengths	154.700, 88.700, 62.600
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.800 - 2.700
R-factor	0.256
Rwork	0.256
R-free	0.28000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1doa
RMSD bond length	0.009
RMSD bond angle	25.000 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (0.5)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.760
High resolution limit [Å]	2.700	2.700
Rmerge	0.062 *	0.434 *
Total number of observations	50106 *
Number of reflections	21165
<I/σ(I)>	13	2.1
Completeness [%]	84.7	80.6
Redundancy	2.36 *	2.28 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.6	20 *	HANGING DROP AT 20C WITH RESERVOIR: 30% PEG 4000, 100 MM NA CITRATE PH=5.6, 5 MM MGCL2, 200 MM AMMONIUM ACETATE, pH 5.60

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	8-10 (mg/ml)
2	1	reservoir	PEG4000	30 (%)
3	1	reservoir	sodium citrate	100 (mM)
4	1	reservoir		5 (mM)
5	1	reservoir	ammonium acetate	200 (mM)