4QT4

Crystal structure of Peptidyl-tRNA hydrolase from a Gram-positive bacterium, Streptococcus pyogenes at 2.19 Angstrom resolution shows the Closed Structure of the Substrate Binding Cleft

Replaces:  4Q55

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	2013-11-26
Detector	MARRESEARCH
Wavelength(s)	0.97
Spacegroup name	P 1
Unit cell lengths	36.024, 43.028, 65.100
Unit cell angles	90.33, 105.78, 112.51

Refinement procedure

Resolution	35.370 - 2.190
R-factor	0.17002
Rwork	0.168
R-free	0.19847
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4jc4
RMSD bond length	0.014
RMSD bond angle	1.589
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC (5.7.0032)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	35.370	2.230
High resolution limit [Å]	2.190	2.190
Number of reflections	17325
<I/σ(I)>	22.2	7.6
Completeness [%]	98.3	97.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP			VAPOR DIFFUSION, HANGING DROP