4DQ6
Crystal structure of PLP-bound putative aminotransferase from Clostridium difficile 630
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 | 2011-07-06 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97718 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 79.426, 56.094, 85.275 |
| Unit cell angles | 90.00, 99.33, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.500 |
| R-factor | 0.1542 |
| Rwork | 0.152 |
| R-free | 0.18620 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4dgt |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.815 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.530 |
| High resolution limit [Å] | 1.500 | 4.070 | 1.500 |
| Rmerge | 0.072 | 0.048 | 0.493 |
| Number of reflections | 118460 | ||
| <I/σ(I)> | 21.5 | 2.3 | |
| Completeness [%] | 99.5 | 99.8 | 93.6 |
| Redundancy | 4 | 4.1 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 293 | Protein: 0.3M NaCl, 10mM Hepes pH 7.5. Precipitant: 25%PEG 2K MME, 0.2M Na Chloride, 0.1M Na Citrate, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
