4RZ5
Transaldolase B E96Q from E.coli
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-11-14 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9763 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 66.760, 90.240, 131.890 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.920 - 1.800 |
| R-factor | 0.21079 |
| Rwork | 0.208 |
| R-free | 0.26216 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1onr monomer |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.295 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.920 | 1.840 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.110 | 0.460 |
| Number of reflections | 74166 | |
| <I/σ(I)> | 5.3 | 1.8 |
| Completeness [%] | 99.5 | 99.7 |
| Redundancy | 4.4 | 4.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293.2 | 0.15M Li2SO4, 23% PEG 3350, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293.2K |
