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 |