2X71
Structural basis for the interaction of lactivicins with serine beta- lactamases
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM30A |
| Synchrotron site | ESRF |
| Beamline | BM30A |
| Temperature [K] | 100 |
| Collection date | 2008-10-15 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 46.652, 104.089, 62.838 |
| Unit cell angles | 90.00, 94.45, 90.00 |
Refinement procedure
| Resolution | 34.690 - 2.100 |
| R-factor | 0.18876 |
| Rwork | 0.187 |
| R-free | 0.22698 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2wk0 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.239 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 34.700 | 2.210 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.110 | 0.390 |
| Number of reflections | 34702 | |
| <I/σ(I)> | 10.8 | 2.5 |
| Completeness [%] | 99.3 | 98.9 |
| Redundancy | 3.6 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 4 | pH 4 |
