7NU4

Crystal Structure of Neisseria gonorrhoeae LeuRS

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE MASSIF-3
Synchrotron site	ESRF
Beamline	MASSIF-3
Temperature [K]	100
Detector technology	PIXEL
Collection date	2018-12-02
Detector	DECTRIS EIGER X 4M
Wavelength(s)	0.967700
Spacegroup name	P 21 21 21
Unit cell lengths	48.778, 81.904, 224.879
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	56.220 - 2.180
R-factor	0.1868
Rwork	0.184
R-free	0.24530
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	6q89
Data reduction software	XDS
Data scaling software	Aimless (0.7.2)
Phasing software	PHASER
Refinement software	PHENIX (1.17.1_3660)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	74.960	74.960	2.200
High resolution limit [Å]	2.090	6.590	2.090
Rmerge	0.119	0.035	1.265
Rmeas	0.128	0.038	1.355
Rpim	0.046	0.014	0.482
Total number of observations	410661	13243	61487
Number of reflections	54838	1946	7892
<I/σ(I)>	10.9	35.4	1.5
Completeness [%]	99.9	99.5	100
Redundancy	7.5	6.8	7.8
CC(1/2)	0.998	0.999	0.720

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5	293	Holo protein at 10 mg/mL in 10 mM Tris pH 7, 100 mM NaCl, 2.5 mM 2-mercaptoethanol was mixed with 0.1 M bis-tris propane pH 8.5, 0.1 M MgCl2, 20% (w/v) PEG 3350 and a crystal seed stock in a 0.75:1.0:0.25 (v/v) ratio. The seed stock was prepared in the same crystallization buffer. Suitable crystals were cryo-protected in an equilvalent precipitant solution supplemented with 22% (v/v) ethylene glycol.