4GAC
High resolution structure of mouse aldehyde reductase (AKR1a4) in its apo-form
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-07-15 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.033 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 56.940, 92.620, 70.100 |
| Unit cell angles | 90.00, 106.16, 90.00 |
Refinement procedure
| Resolution | 19.733 - 1.640 |
| R-factor | 0.1495 |
| Rwork | 0.148 |
| R-free | 0.17840 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2he8 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.119 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | PHENIX (1.7.3_928) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 19.733 | 19.733 | 1.680 |
| High resolution limit [Å] | 1.640 | 7.330 | 1.640 |
| Rmerge | 0.044 | 0.025 | 0.144 |
| Number of reflections | 84168 | 889 | 6163 |
| <I/σ(I)> | 19.7 | 31.57 | 8 |
| Completeness [%] | 98.5 | 88.9 | 97.7 |
| Redundancy | 2.96 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.8 | 295 | 26% PEG-4000, 0.1 M NaCitrate, pH 5.8, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
