5EVB
Crystal structure of the metallo-beta-lactamase L1 in complex with the bisthiazolidine inhibitor D-CS319
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I24 |
| Synchrotron site | Diamond |
| Beamline | I24 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-02-27 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.96862 |
| Spacegroup name | P 64 2 2 |
| Unit cell lengths | 104.957, 104.957, 98.828 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 28.968 - 1.841 |
| R-factor | 0.1501 |
| Rwork | 0.148 |
| R-free | 0.19490 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1sml |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.044 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 28.970 | 1.880 |
| High resolution limit [Å] | 1.840 | 1.840 |
| Rmerge | 0.213 | 0.650 |
| Number of reflections | 28142 | |
| <I/σ(I)> | 16.9 | 6 |
| Completeness [%] | 99.4 | 90.3 |
| Redundancy | 37.9 | 27.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 277.15 | 100 mM Hepes pH 7.75, 2.0 M ammonium sulphate, 1.5% PEG400. 1 ul protein (15 mg/ml) mixed with 1 ul reservoir. |
