2FZN
Structure of the E. coli PutA proline dehydrogenase domain reduced by dithionite and complexed with proline
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 173 |
| Detector technology | CCD |
| Collection date | 2003-11-15 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.97856 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 73.115, 143.221, 145.124 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 22.700 - 2.000 |
| R-factor | 0.216 |
| Rwork | 0.214 |
| R-free | 0.25100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | : 1TJ0 |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.413 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 27.000 | 27.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 4.300 | 2.000 |
| Rmerge | 0.061 | 0.029 | 0.419 |
| Number of reflections | 51335 | 5075 | 4706 |
| <I/σ(I)> | 12.3 | ||
| Completeness [%] | 98.1 | ||
| Redundancy | 5.7 | 5.5 | 4.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.7 | 293 | The crystal was grown in 13-15% PEG 3350, 60-190 mM citrate buffer. Prior to data collection a crystal was soaked in excess Na dithionite and proline in order to reduce the FAD cofactor., pH 5.7, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
