2E0W
T391A precursor mutant protein of gamma-Glutamyltranspeptidase from Escherichia coli
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL41XU |
| Synchrotron site | SPring-8 |
| Beamline | BL41XU |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-04-16 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 134.600, 134.600, 118.400 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.550 |
| R-factor | 0.22 |
| Rwork | 0.217 |
| R-free | 0.27000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | A MOLECULE (CHAIN ID A B) OF PDB ENTRY 2DBU |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.282 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.640 |
| High resolution limit [Å] | 2.550 | 2.550 |
| Rmerge | 0.092 | 0.314 |
| Number of reflections | 33506 | |
| <I/σ(I)> | 11.2 | |
| Completeness [%] | 92.7 | 91.9 |
| Redundancy | 12 | 11.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 277 | 18% PEG 4000, 10% iso-propanol, 0.1M sodium citrate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
