2XK1
Crystal structure of a complex between Actinomadura R39 DD-peptidase and a boronate inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM30A |
| Synchrotron site | ESRF |
| Beamline | BM30A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-01-25 |
| Detector | MARRESEARCH SX-165 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 154.898, 92.348, 143.829 |
| Unit cell angles | 90.00, 92.25, 90.00 |
Refinement procedure
| Resolution | 27.530 - 2.800 |
| R-factor | 0.219 |
| Rwork | 0.217 |
| R-free | 0.26400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2wk0 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.164 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 38.800 | 2.950 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.080 | 0.430 |
| Number of reflections | 49784 | |
| <I/σ(I)> | 12.7 | 2.6 |
| Completeness [%] | 99.4 | 99.5 |
| Redundancy | 3.5 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 |
