6J93

Crystal structure of Peptidyl-tRNA hydrolase from Acinetobacter baumannii at 0.95 A resolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID23-1
Synchrotron site	ESRF
Beamline	ID23-1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2018-12-01
Detector	PSI PILATUS 6M
Wavelength(s)	0.97199
Spacegroup name	P 21 21 21
Unit cell lengths	33.995, 66.257, 76.186
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	33.130 - 0.950
R-factor	0.13374
Rwork	0.134
R-free	0.15278
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5y9a
RMSD bond length	0.018
RMSD bond angle	1.986
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0238)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	33.130	0.970
High resolution limit [Å]	0.950	0.950
Rmerge	0.100	1.420
Rmeas	0.100
Rpim	0.034	0.630
Number of reflections	97251	10028
<I/σ(I)>	9.7	0.45
Completeness [%]	88.9
Redundancy	8.8	3.802
CC(1/2)	0.990	0.400

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	298	12% PEG 1500, 0.1M HEPES, pH 7.5, 20% Glycerol