8C3N

Stapled peptide SP30 in complex with humanised RadA mutant HumRadA22

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I04
Synchrotron site	Diamond
Beamline	I04
Temperature [K]	100
Detector technology	PIXEL
Collection date	2021-03-04
Detector	DECTRIS EIGER2 X 16M
Wavelength(s)	0.9795
Spacegroup name	P 21 21 2
Unit cell lengths	143.017, 37.961, 43.934
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	37.430 - 1.210
R-factor	0.211
Rwork	0.211
R-free	0.21820
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	6hqu
RMSD bond length	0.038
RMSD bond angle	2.063
Data reduction software	autoPROC
Data scaling software	autoPROC
Phasing software	PHASER
Refinement software	BUSTER

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	37.430	1.230
High resolution limit [Å]	1.210	1.210
Rmeas	0.053
Number of reflections	70100	2237
<I/σ(I)>	13.6	0.5
Completeness [%]	94.9
Redundancy	6.9
CC(1/2)	1.000	0.400

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	Protein: 0.5 mM SP30:HumRadA22 in 20 mM CHES pH 9.5, 100 mM NaCl, 20 mM ADP/MgCl 2 Condition: 14% w/v PEG 4000 (precipitant), 6% v/v MPD (precipitant), 0.1M Na K Phos pH 6.2 (buffer)