9QQ7

Crystal structure of the relaxase domain of RelpLS20, Se-Met derivative

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALBA BEAMLINE XALOC
Synchrotron site	ALBA
Beamline	XALOC
Temperature [K]	100
Detector technology	PIXEL
Collection date	2016-02-05
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.979190
Spacegroup name	P 61
Unit cell lengths	102.054, 102.054, 59.116
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	19.310 - 1.800
R-factor	0.1841
Rwork	0.183
R-free	0.21050
Structure solution method	SAD
RMSD bond length	0.015
RMSD bond angle	1.375
Data reduction software	XDS (20221120)
Data scaling software	XSCALE (20221120)
Phasing software	SHELXCD (2016/1)
Refinement software	PHENIX (1.20.1_4487)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	19.310	7.110	1.630
High resolution limit [Å]	1.590	5.020	1.590
Rmerge	0.056	0.036	3.025
Rmeas	0.060	0.038	3.272
Number of reflections	63980	993	3508
<I/σ(I)>	12.9
Completeness [%]	99.6
Redundancy	4.31
CC(1/2)	0.999	0.998	0.178

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8	291	1ul of protein at 6mg/ml in 20mM Tris pH 8.0, 500mM NaCl were added to 1ul reservoir (0.1 M Imidazole pH 8.0, 10 % PEG 8000) and equilibrated against 100 uL of the crystallization buffer. Bar-shaped crystals took 16 h to grow to the maximum size at 18 C. Cryo-cooling in liquid nitrogen was carried out using a cryo-protecting solution containing reservoir solution supplemented with 20 % (w/v) glycerol.