9LKP
X-ray structure of Enterobacter cloaca transaldolase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-5A |
| Synchrotron site | Photon Factory |
| Beamline | BL-5A |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-06-03 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1.0 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 99.000, 180.070, 134.040 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.480 - 1.630 |
| R-factor | 0.17451 |
| Rwork | 0.173 |
| R-free | 0.19735 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3s1v |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.203 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0430) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.680 | 1.670 |
| High resolution limit [Å] | 1.630 | 1.630 |
| Rmerge | 0.068 | 0.913 |
| Number of reflections | 148396 | 10888 |
| <I/σ(I)> | 17.6 | 2.1 |
| Completeness [%] | 99.9 | |
| Redundancy | 6.5 | |
| CC(1/2) | 0.999 | 0.736 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 298 | 100 mM cacodylate buffer, pH 6.5, 10% (w/v) PEG3000, 10% (w/v) PEG 8000, 200 mM of MgCl2 |
