3R8R
Transaldolase from Bacillus subtilis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I711 |
| Synchrotron site | MAX II |
| Beamline | I711 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2004-11-13 |
| Detector | MAR scanner 345 mm plate |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 143.299, 127.280, 158.448 |
| Unit cell angles | 90.00, 98.10, 90.00 |
Refinement procedure
| Resolution | 58.930 - 1.900 |
| R-factor | 0.202 |
| Rwork | 0.200 |
| R-free | 0.22900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1l6w |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.131 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 69.000 | 2.000 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.087 | 0.525 |
| Number of reflections | 441576 | |
| <I/σ(I)> | 10.6 | 2.4 |
| Completeness [%] | 100.0 | 99.9 |
| Redundancy | 3.5 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 9 | 293 | 20% PEG 4K, 0.2M of Li2SO4, 20% of glycerol, 100 mM Tris/HCl, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
