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 |