1NRF
C-terminal domain of the Bacillus licheniformis BlaR penicillin-receptor
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 | 2002-09-07 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.9786 |
| Spacegroup name | P 41 |
| Unit cell lengths | 45.848, 45.848, 130.198 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 31.500 * - 2.500 |
| Rwork | 0.204 |
| R-free | 0.25700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Class D beta-lactamase OXA-2 from Salmonella typhimurium |
| RMSD bond length | 0.007 |
| RMSD bond angle | 23.100 * |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 32.440 * | 2.500 |
| High resolution limit [Å] | 2.440 | 2.440 |
| Rmerge | 0.068 * | 0.232 |
| Number of reflections | 9979 | 745 * |
| <I/σ(I)> | 8.9 | 3.7 |
| Completeness [%] | 99.7 | 99.9 * |
| Redundancy | 4 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.95 | 293 | 18% PEG 8000, 5% Glycerol, 50mM CaCl2 in 0.1M Cacodylate, pH 6.95, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 20 (mg/ml) | |
| 2 | 1 | reservoir | PEG8000 | 18 (%) | |
| 3 | 1 | reservoir | glycerol | 5 (%) | |
| 4 | 1 | reservoir | 50 (mM) | ||
| 5 | 1 | reservoir | cacodylate | 0.1 (M) | pH6.95 |
