5E3I

Crystal Structure of a Histidyl-tRNA synthetase from Acinetobacter baumannii with bound L-Histidine and ATP

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	2015-04-21
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.97872
Spacegroup name	I 2 2 2
Unit cell lengths	88.810, 103.070, 246.300
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	47.540 - 2.200
R-factor	0.1661
Rwork	0.165
R-free	0.20540
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1kmm
RMSD bond length	0.007
RMSD bond angle	0.910
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	BALBES
Refinement software	PHENIX (1.10_2155)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.260
High resolution limit [Å]	2.200	9.840	2.200
Rmerge	0.077	0.029	0.533
Rmeas	0.084	0.032	0.580
Total number of observations	352039
Number of reflections	57675	696	4195
<I/σ(I)>	15.55	32.7	3.79
Completeness [%]	99.9	94.6	100
Redundancy	6.1		6.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		290	AcbaC.00063.a.B1.PW37682 at 19.5 mg/ml incubated with 3 mM L-Histidine, ATP, and MgCl2, then then mixed 1:1 with MCSG1(e3): 50mM MgCl2, 0.1M Hepes, pH=7.5, 30% PEG-MME550, cryoprotected with 20% ethylene glycol