2JFG
Crystal structure of MurD ligase in complex with UMA and ADP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 288 |
| Detector technology | CCD |
| Collection date | 2006-10-02 |
| Detector | ADSC CCD |
| Spacegroup name | P 41 |
| Unit cell lengths | 65.085, 65.085, 134.253 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 65.090 - 1.520 |
| R-factor | 0.189 |
| Rwork | 0.188 |
| R-free | 0.21500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3uag |
| RMSD bond length | 0.043 |
| RMSD bond angle | 1.590 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 65.000 | 1.610 |
| High resolution limit [Å] | 1.520 | 1.520 |
| Rmerge | 0.040 | 0.300 |
| Number of reflections | 82385 | |
| <I/σ(I)> | 31 | 5.7 |
| Completeness [%] | 96.3 | 91.5 |
| Redundancy | 4.6 | 4.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | PROTEIN WAS CRYSTALLIZED FROM 1.7 M (NH4)2SO4, 7% PEG 400, 100 MM HEPES, PH 7.5 |
