6WOM

Crystal structure of Aspartyl-tRNA ligase from Elizabethkingia sp.

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	2017-10-18
Detector	RAYONIX MX-300
Wavelength(s)	0.97856
Spacegroup name	C 1 2 1
Unit cell lengths	234.370, 106.570, 93.410
Unit cell angles	90.00, 100.91, 90.00

Refinement procedure

Resolution	36.070 - 2.150
R-factor	0.1878
Rwork	0.187
R-free	0.22530
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1g51A as per MorDA
RMSD bond length	0.008
RMSD bond angle	0.877
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MoRDa
Refinement software	PHENIX (1.18rc7 3834)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	36.070	36.070	2.210
High resolution limit [Å]	2.150	9.620	2.150
Rmerge	0.052	0.020	0.575
Rmeas	0.061	0.023	0.669
Total number of observations	465254
Number of reflections	120694	1369	8815
<I/σ(I)>	16.86	47.55	2.37
Completeness [%]	98.5	94.7	97.5
Redundancy	3.855	3.428	3.815
CC(1/2)	0.999	0.999	0.791

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.6	290	Anatrace/Microlytic MGSG1 screen, condition C8: 25% (w/V) PEG 4000, 200mM Ammonium sulfate, 100mM sodium citrate tribasic / HCl pH 5.6: ElmeA.00145.a.B1.PW38328 at 22.48mg/ml: tray: 295094c8: cryo: 15% EG, puck tcq3-6. Subunit C has few crystal lattice contactsleading to poor electron density.