6WBD

Crystal Structure of Lysyl-tRNA synthetase from Stenotrophomonas maltophilia with bound L-lysine

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2020-02-13
Detector	RAYONIX MX-300
Wavelength(s)	0.97872
Spacegroup name	P 31 2 1
Unit cell lengths	127.160, 127.160, 158.700
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	41.620 - 2.050
R-factor	0.1514
Rwork	0.149
R-free	0.18390
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1bbu
RMSD bond length	0.007
RMSD bond angle	0.805
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MoRDa
Refinement software	PHENIX (1.17.1-3360)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.100
High resolution limit [Å]	2.050	9.170	2.050
Rmerge	0.080	0.032	0.560
Rmeas	0.085	0.035	0.600
Number of reflections	87130	978	6522
<I/σ(I)>	17.32	49.58	3.4
Completeness [%]	93.3	83.4	95.6
Redundancy	8.035	7.668	7.897
CC(1/2)	0.999	0.999	0.878

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	287	StmaA.00612.a.B1.PW38745 at 10 mg/ml was incubated with 2 mM L-lysine and adenosine, then mixed 1:1 with Morpheus(H6): 10% (w/v) PEG 8000, 20% (v/v) ethylene glycol, 0.1 M MOPS/HEPES-Na pH 7.5, 0.02 M each sodium L-glutamate, DL-alanine, glycine, DL-lysine HCl, DL-serine. Tray 313975h6. Puck xdi4-1.