1TIW
Crystal structure of E. coli PutA proline dehydrogenase domain (residues 86-669) complexed with L-Tetrahydro-2-furoic acid
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 | CUSTOM-MADE |
| Wavelength(s) | 0.97856 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 72.588, 141.358, 145.897 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 24.840 - 2.000 |
| R-factor | 0.21565 |
| Rwork | 0.214 |
| R-free | 0.25262 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1K87 |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.396 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 99.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.068 | 0.352 |
| Number of reflections | 49933 | |
| <I/σ(I)> | 24 | 4.2 |
| Completeness [%] | 98.0 | 91 |
| Redundancy | 7.9 | 6.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.7 | 295 | 13-15% PEG 3000 or PEG 3350, 60-190 mM citrate, pH 5.7, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
