8QDF

Engineered LmrR with Met-89 replaced by para-boronophenylalanine

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE MASSIF-1
Synchrotron site	ESRF
Beamline	MASSIF-1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2022-11-05
Detector	DECTRIS PILATUS3 6M
Wavelength(s)	0.96546
Spacegroup name	P 1 21 1
Unit cell lengths	60.674, 53.890, 69.034
Unit cell angles	90.00, 95.45, 90.00

Refinement procedure

Resolution	43.370 - 2.200
R-factor	0.2101
Rwork	0.206
R-free	0.27740
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.014
RMSD bond angle	1.322
Data reduction software	xia2 (3.8.6)
Data scaling software	Aimless (0.7.9)
Phasing software	PHASER (2.8.3)
Refinement software	PHENIX ((1.20rc1_4395: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	53.890	2.270
High resolution limit [Å]	2.200	2.200
Rmerge	0.082	0.376
Rmeas	0.099	0.456
Rpim	0.056	0.254
Total number of observations	70024	6099
Number of reflections	22769	1970
<I/σ(I)>	6.8	2.3
Completeness [%]	99.7
Redundancy	3.1	3.1
CC(1/2)	0.991	0.812

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6	293	Protein was concentrated to 9 mg/ml in 20 mM Tris-HCl, pH 8.0, 280 mM NaCl and 1 mM EDTA. Reservoir solution contained 25% PEG 1500 in 0.1 M malonate/imidazole/boric acid buffer, pH 6.0