2VTZ
Biosynthetic thiolase from Z. ramigera. Complex of the C89A mutant with coenzyme A.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X13 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X13 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 84.220, 79.570, 148.920 |
| Unit cell angles | 90.00, 92.10, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.300 |
| R-factor | 0.22407 |
| Rwork | 0.222 |
| R-free | 0.26245 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1m3z |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.127 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.400 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.070 | 0.270 |
| Number of reflections | 87692 | |
| <I/σ(I)> | 15.6 | 4.8 |
| Completeness [%] | 97.2 | 86.1 |
| Redundancy | 3.5 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5 | pH 5 |
