9RFF

Crystal Structure of Human Rac1 Fused with the Scaffold Protein POSH (residues 319-371)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE MASSIF-1
Synchrotron site	ESRF
Beamline	MASSIF-1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2022-11-13
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.9655
Spacegroup name	P 21 21 21
Unit cell lengths	39.222, 73.082, 73.283
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	51.748 - 1.248
Rwork	0.134
R-free	0.16400
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.012
RMSD bond angle	1.783
Data reduction software	autoPROC (1.1.7 (20211020))
Data scaling software	autoPROC (1.1.7 (20211020))
Phasing software	PHASER
Refinement software	REFMAC (5.8.0425)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	51.750	1.337
High resolution limit [Å]	1.248	1.248
Rmerge	0.088	1.500
Rmeas	0.092
Rpim	0.026	0.500
Number of reflections	50198	2510
<I/σ(I)>	14.9	1.4
Completeness [%]	95.0	56
Redundancy	12.9	11.8
CC(1/2)	0.999	0.576

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	277	0.12 M ethylene glycol, 0.1 M imidazole-MES pH 6.5, 37% (v/v) 2-methyl-2,4-pentanediol (MPD)-PEG 1000-PEG 3500 2 mg/mL Rac1-POSH