8CNJ

HRas(1-166) in complex with GDP and BeF3-

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I03
Synchrotron site	Diamond
Beamline	I03
Temperature [K]	100
Detector technology	PIXEL
Collection date	2023-02-18
Detector	DECTRIS EIGER2 X 16M
Wavelength(s)	0.9763
Spacegroup name	P 21 21 21
Unit cell lengths	45.433, 51.957, 136.149
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.589 - 1.350
Rwork	0.143
R-free	0.17910
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.011
RMSD bond angle	1.412
Data reduction software	DIALS
Data scaling software	Aimless
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0405)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	51.960	51.960	1.370
High resolution limit [Å]	1.350	7.390	1.350
Rmerge	0.093	0.035	1.532
Rmeas	0.100	0.037	1.712
Rpim	0.038	0.014	0.743
Number of reflections	69077	533	2387
<I/σ(I)>	13.7
Completeness [%]	96.2
Redundancy	12.6	11.8	8.6
CC(1/2)	0.999	0.999	0.598

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		277	BeF3- GSA complexes were obtained under vapour diffusion sitting drop conditions. Protein buffer (HRas pY64 or HRas 0.4 mM, Na-HEPES 20 mM pH = 8.0, MgCl2 5 mM, NaF 20 mM) were mixed with precipitant in a 1:1 ratio with a total drop size of 600 nL. The precipitant solution consited of: (30 % (v/v) MPD, 100 mM imidazole, pH = 7.0). Protein crystals were soaked in their respective precipitant solutions containing 50 mM BeCl2 and subsequently flash-frozen using 20% glycerol as cryoprotectant.