3AHH
H142A mutant of Phosphoketolase from Bifidobacterium Breve complexed with acetyl 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 | 2009-12-02 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.0000 |
| Spacegroup name | I 4 2 2 |
| Unit cell lengths | 174.606, 174.606, 163.644 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 34.150 - 2.100 |
| R-factor | 0.16026 |
| Rwork | 0.158 |
| R-free | 0.19630 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3ahc |
| RMSD bond length | 0.029 |
| RMSD bond angle | 2.139 |
| 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 | 2.140 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.072 | 0.284 |
| Number of reflections | 73374 | |
| <I/σ(I)> | 44.7 | 9.7 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 14.7 | 14.9 |
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 |
