1ONH
GC1 beta-lactamase with a penem inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CHESS BEAMLINE A1 |
| Synchrotron site | CHESS |
| Beamline | A1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-06-24 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.9474 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 76.288, 68.873, 62.014 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.380 |
| R-factor | 0.1383 |
| Rwork | 0.135 |
| R-free | 0.20200 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1gce |
| RMSD bond length | 0.010 |
| RMSD bond angle | 0.028 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.430 |
| High resolution limit [Å] | 1.380 | 1.380 |
| Rmerge | 0.103 | 0.514 |
| Total number of observations | 377696 * | |
| Number of reflections | 65047 | 5075 * |
| <I/σ(I)> | 10.5 | 2 |
| Completeness [%] | 97.2 | 77 |
| Redundancy | 5.8 | 2.52 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 293 | 10% PEG 8000 in 50 mM HEPES over 20 % PEG, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | PEG8000 | 10 (%) | |
| 3 | 1 | drop | HEPES | 50 (mM) | pH7.0 |
| 4 | 1 | reservoir | PEG | 20 (%) | |
| 5 | 1 | reservoir | HEPES | 100 (mM) |
