7N12

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	CLSI BEAMLINE 08B1-1
Synchrotron site	CLSI
Beamline	08B1-1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2021-02-28
Detector	DECTRIS PILATUS3 6M
Wavelength(s)	1.52131
Spacegroup name	C 1 2 1
Unit cell lengths	113.439, 37.107, 100.287
Unit cell angles	90.00, 112.28, 90.00

Refinement procedure

Resolution	92.800 - 1.700
R-factor	0.1861
Rwork	0.184
R-free	0.22670
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5agr
RMSD bond length	0.013
RMSD bond angle	1.216
Data reduction software	DIALS (3.4.3)
Data scaling software	DIALS (3.4.3)
Phasing software	PHASER (1.15.2_3472)
Refinement software	PHENIX (1.15.2_3472)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	92.970	1.750
High resolution limit [Å]	1.520	1.710
Rmerge		0.457
Rmeas	0.110	0.506
Rpim	0.044	0.214
Number of reflections	56594	2931
<I/σ(I)>	7.7	1.4
Completeness [%]	94.2	99.57
Redundancy	5.5	5.35
CC(1/2)		0.833

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	293	2 ul 7.5 mg/ml protein solution (50 mM Tris pH 7.5, 150 mM NaCl. 2 mM BME) was mixed with crystallization solution (100 mM HEPES, pH 7.5, 2% PEG400, 2.1 M ammonium sulfate, 10 mM AMP, 1 mM epetraborole, 15% glycerol)