3G9K
Crystal structure of Bacillus anthracis transpeptidase enzyme CapD
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-12-19 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9794 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 52.668, 120.621, 77.375 |
| Unit cell angles | 90.00, 90.87, 90.00 |
Refinement procedure
| Resolution | 40.690 - 1.790 |
| R-factor | 0.19875 |
| Rwork | 0.197 |
| R-free | 0.24166 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3ga9 |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.587 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.830 |
| High resolution limit [Å] | 1.790 | 1.790 |
| Rmerge | 0.117 | 0.555 |
| Number of reflections | 83551 | |
| <I/σ(I)> | 16.1 | 1.73 |
| Completeness [%] | 98.0 | 82.9 |
| Redundancy | 4.7 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 298 | 15% PEG 3350, 8% PEG 400, 0.05M LiSO4, 0.1M Na-Hepes pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
