7N11

Crystal structure of the M. abscessus LeuRS editing domain in complex with epetraborole-AMP adduct

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 24-ID-E
Synchrotron site	APS
Beamline	24-ID-E
Temperature [K]	100
Detector technology	PIXEL
Collection date	2020-10-21
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.979
Spacegroup name	P 21 2 21
Unit cell lengths	37.249, 51.597, 116.149
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	38.570 - 2.100
R-factor	0.1882
Rwork	0.184
R-free	0.22580
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5agr
RMSD bond length	0.008
RMSD bond angle	0.999
Data reduction software	HKL-2000 (v720)
Data scaling software	HKL-2000 (v720)
Phasing software	PHASER (1.15.2_3472)
Refinement software	PHENIX (1.15.2_3472)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.720
High resolution limit [Å]	1.690	1.690
Rmeas	0.281	1.166
Rpim	0.095	0.824
Number of reflections	25482	66
<I/σ(I)>	4.4
Completeness [%]	76.8
Redundancy	6.8	5.5
CC(1/2)	0.974

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	293	2 ul of 10 mg/ml protein solution (50 mM Tris pH 7.5, 150 mM NaCl, 2 mM BME) were mixed with 2 ul of crystallization solution (100 mM HEPES pH 7.0, 2.5 M ammonium sulfate)