2E1D
Crystal structure of mouse transaldolase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 93 |
| Detector technology | CCD |
| Collection date | 2005-09-05 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97243 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 51.984, 107.488, 60.877 |
| Unit cell angles | 90.00, 96.91, 90.00 |
Refinement procedure
| Resolution | 46.520 - 2.000 |
| R-factor | 0.169 |
| Rwork | 0.169 |
| R-free | 0.21100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1f05 |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.100 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.090 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Number of reflections | 44262 | |
| <I/σ(I)> | 34.3 | 6.95 |
| Completeness [%] | 99.4 | 97.6 |
| Redundancy | 7.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 0.1M MES, 21% PEG3350, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
