3AHG
H64A mutant of Phosphoketolase from Bifidobacterium Breve complexed with a tricyclic ring form of thiamine diphosphate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-5A |
| Synchrotron site | Photon Factory |
| Beamline | BL-5A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-10-19 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.0000 |
| Spacegroup name | I 4 2 2 |
| Unit cell lengths | 175.035, 175.035, 163.597 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 33.500 - 1.900 |
| R-factor | 0.16542 |
| Rwork | 0.163 |
| R-free | 0.20546 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3ahc |
| RMSD bond length | 0.031 |
| RMSD bond angle | 2.221 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | REFMAC (5.5.0102) |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.930 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.058 | 0.311 |
| Number of reflections | 98341 | |
| <I/σ(I)> | 57.6 | 8.8 |
| Completeness [%] | 99.3 | 100 |
| Redundancy | 13.9 | 12.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 9 | 293 | 24%(v/v) PEG 6000, 0.1M BICINE buffer, pH 9.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
