6JGU

Crystal structure at atomic resolution reveals the catalytic mechanism in peptidyl-tRNA hydrolase from Acinetobacter baumannii.

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	33.964, 66.194, 75.983
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	49.910 - 1.020
R-factor	0.13772
Rwork	0.137
R-free	0.15726
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5y9a
RMSD bond length	0.018
RMSD bond angle	1.897
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]	49.920	1.049
High resolution limit [Å]	1.020	1.022
Rmerge	0.093	2.236
Rpim	0.039	0.983
Number of reflections	73420	6369
<I/σ(I)>	8.45	0.756
Completeness [%]	88.4
Redundancy	8.3
CC(1/2)	0.998	0.243

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	298	12% PEG 1500, 0.1M HEPES (4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid), pH 7.5, 20% Glycerol