2CWN
Crystal structure of mouse transaldolase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL26B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL26B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-05-26 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 79.050, 108.009, 75.608 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.980 - 2.100 |
| R-factor | 0.196 |
| Rwork | 0.196 |
| R-free | 0.23900 |
| 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 | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.180 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Number of reflections | 38360 | |
| <I/σ(I)> | 15.1 | 3.3 |
| Completeness [%] | 99.0 | 93.8 |
| Redundancy | 5.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.7 | 293 | Bis-Tris, PEG3350, pH 5.7, VAPOR DIFFUSION, SITTING DROP, temperature 293K |






