2PTH
PEPTIDYL-TRNA HYDROLASE FROM ESCHERICHIA COLI
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | LURE BEAMLINE DW32 |
| Synchrotron site | LURE |
| Beamline | DW32 |
| Temperature [K] | 273 |
| Detector technology | IMAGE PLATE |
| Collection date | 1996-02 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 47.240, 63.590, 62.570 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 1.200 |
| R-factor | 0.196 |
| Rwork | 0.196 |
| R-free | 0.21500 |
| Structure solution method | MULTIPLE ISOMORPHOUS REPLACEMENTS |
| RMSD bond length | 0.008 |
| RMSD bond angle | 22.500 * |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | X-PLOR (3.1) |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 28.000 | 1.230 |
| High resolution limit [Å] | 1.200 | 1.200 |
| Rmerge | 0.046 * | |
| Number of reflections | 55575 | |
| <I/σ(I)> | 8.3 | 4.6 |
| Completeness [%] | 93.9 | 85.3 |
| Redundancy | 4.2 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 | 6 * | Schmitt, E., (1997) Proteins.Struct.Funct.Genet., 28, 135. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | PEG6000 | 10-12 (%) | |
| 2 | 1 | reservoir | isopropanol | 12 (%) | |
| 3 | 1 | reservoir | Tris-HCl | 0.1 (M) | |
| 4 | 1 | drop | protein | 2 (mg/ml) |
