3P2J
Crystal structure of peptidyl-tRNA hydrolase from Mycobacterium smegmatis at 2.2 A resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 298 |
Detector technology | IMAGE PLATE |
Collection date | 2009-05-26 |
Detector | MARRESEARCH |
Wavelength(s) | 1.514 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 44.909, 58.943, 61.854 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 14.960 - 2.220 |
R-factor | 0.19293 |
Rwork | 0.192 |
R-free | 0.21818 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3kjz |
RMSD bond length | 0.013 |
RMSD bond angle | 1.707 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 42.670 | 2.300 |
High resolution limit [Å] | 2.220 | 2.220 |
Number of reflections | 8170 | |
<I/σ(I)> | 11.9 | 2 |
Completeness [%] | 95.6 | 89.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 20mM Tris-HCl, 1mM EDTA, 50mM NaCl, 10% isopropanol, 30% PEG 1500, 5mM 2-mercaptoethanol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |