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: 4Q55Experimental 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 |
