2Y3Z
Structure of Isopropylmalate dehydrogenase from Thermus thermophilus - apo enzyme
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC CCD |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 76.480, 76.480, 154.300 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 40.000 - 1.830 |
| R-factor | 0.16525 |
| Rwork | 0.164 |
| R-free | 0.19698 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1hex |
| RMSD bond length | 0.022 |
| RMSD bond angle | 1.852 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 99.000 | 1.860 |
| High resolution limit [Å] | 1.830 | 1.830 |
| Rmerge | 0.080 | 0.650 |
| Number of reflections | 47324 | |
| <I/σ(I)> | 16.7 | 2.4 |
| Completeness [%] | 99.0 | 91.2 |
| Redundancy | 6 | 4.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 9 | 35% PEG-550-MME, 0.1 M TRIS-HCL PH 9.0, 0.1 M NACL |
