6A31

Crystal structure of Na+ bound Peptidyl-tRNA Hydrolase from Acinetobacter baumannii at 2.19 A resolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM14
Synchrotron site	ESRF
Beamline	BM14
Temperature [K]	300
Detector technology	PIXEL
Collection date	2018-05-13
Detector	DECTRIS PILATUS3 6M
Wavelength(s)	0.9537
Spacegroup name	P 21 2 21
Unit cell lengths	34.290, 58.750, 109.210
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	54.600 - 2.190
R-factor	0.17708
Rwork	0.174
R-free	0.23406
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4jy7
RMSD bond length	0.016
RMSD bond angle	1.732
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC (5.8.0158)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	54.600	2.230
High resolution limit [Å]	2.190	2.190
Rmerge	0.165	0.800
Rmeas	0.176	0.935
Rpim	0.058	0.301
Number of reflections	11810	11810
<I/σ(I)>	8.7	2.2
Completeness [%]	98.7	97
Redundancy	9.1	9.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	298	100 mM NaHEPES pH 7.5 25% PEG 1500