5LGE
Crystal Structure of human IDH1 mutant (R132H) in complex with NADP+ and an Inhibitor related to BAY 1436032
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 93 |
| Detector technology | PIXEL |
| Collection date | 2013-12-16 |
| Detector | DECTRIS PILATUS 6M-F |
| Wavelength(s) | 0.976 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 96.900, 110.320, 198.540 |
| Unit cell angles | 90.00, 91.19, 90.00 |
Refinement procedure
| Resolution | 29.940 - 2.700 |
| R-factor | 0.19722 |
| Rwork | 0.195 |
| R-free | 0.22977 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4kzo |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.484 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.850 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.120 | 0.700 |
| Number of reflections | 56625 | |
| <I/σ(I)> | 8.6 | 2.3 |
| Completeness [%] | 98.7 | 99 |
| Redundancy | 4.8 | 4.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 7 | 293 | PROTEIN BUFFER: 15 MG/ML. PROTEIN IN 25 MM HEPES, 300 MM NACL, 5 MM BETA-ME, COMPLETE PROTEASE INHIBITOR MIXTURE, PH 7.7 RESERVOIR: 100 MM BIS-TRIS, PH 7.0, 200 MM CA-ACETATE, 20.0 %(W/V) PEG 3350 |
