5Y98

Crystal structure of native unbound peptidyl tRNA hydrolase from Acinetobacter baumannii at 1.36 A resolution

Replaces:  3WH4

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM14
Synchrotron site	ESRF
Beamline	BM14
Temperature [K]	100
Detector technology	CCD
Collection date	2013-06-23
Detector	MARRESEARCH
Wavelength(s)	0.97
Spacegroup name	P 21 21 21
Unit cell lengths	33.980, 65.970, 75.880
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	25.320 - 1.360
R-factor	0.10807
Rwork	0.106
R-free	0.14449
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3WH4
RMSD bond length	0.031
RMSD bond angle	2.210
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0135)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.320	1.395
High resolution limit [Å]	1.360	1.360
Number of reflections	37477
<I/σ(I)>	20.2
Completeness [%]	99.9
Redundancy	4.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	298	50mM HEPES, PEG 400, PEG 1500, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K