3TG9
The crystal structure of penicillin binding protein from Bacillus halodurans
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X29A |
| Synchrotron site | NSLS |
| Beamline | X29A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-02-07 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 65.241, 79.800, 74.443 |
| Unit cell angles | 90.00, 100.49, 90.00 |
Refinement procedure
| Resolution | 49.999 - 2.200 |
| R-factor | 0.1948 |
| Rwork | 0.193 |
| R-free | 0.23050 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2qmi |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.038 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.280 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.067 | 0.248 |
| Number of reflections | 38211 | |
| <I/σ(I)> | 20.4 | 5.5 |
| Completeness [%] | 99.9 | 99.2 |
| Redundancy | 4.9 | 4.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 293 | 0.2 M Ammonium sulfate, 0.1 M BIS-TRIS pH 5.5, 25% w/v Polyethylene glycol 3,350, 0.8% 1,4- butanediol, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
