4LWQ

Crystal structure of native peptidyl t-RNA hydrolase from Acinetobacter baumannii at 1.38A resolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM14
Synchrotron site	ESRF
Beamline	BM14
Temperature [K]	77
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, 65.980, 75.890
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	25.310 - 1.380
R-factor	0.13091
Rwork	0.130
R-free	0.15242
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4jwk
RMSD bond length	0.007
RMSD bond angle	1.117
Data reduction software	MOSFLM
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC (5.7.0032)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.310	1.400
High resolution limit [Å]	1.380	1.380
Number of reflections	34019
Completeness [%]	100.0	97.9

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