5TC4
Crystal structure of human mitochondrial methylenetetrahydrofolate dehydrogenase-cyclohydrolase (MTHFD2) in complex with LY345899 and cofactors
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE MASSIF-3 |
| Synchrotron site | ESRF |
| Beamline | MASSIF-3 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-09-03 |
| Detector | DECTRIS PILATUS 2M |
| Wavelength(s) | 0.9677 |
| Spacegroup name | I 4 |
| Unit cell lengths | 74.323, 74.323, 98.620 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 37.160 - 1.890 |
| R-factor | 0.16509 |
| Rwork | 0.163 |
| R-free | 0.21222 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1b0a |
| RMSD bond length | 0.023 |
| RMSD bond angle | 2.276 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 37.160 | 1.930 |
| High resolution limit [Å] | 1.890 | 1.890 |
| Rmerge | 0.316 | 4.348 |
| Number of reflections | 21322 | |
| <I/σ(I)> | 6.8 | 0.9 |
| Completeness [%] | 99.8 | 96.8 |
| Redundancy | 6.9 | 6.7 |
| CC(1/2) | 0.980 | 0.297 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.1 M Phosphate/Citrate pH 4.1, 38 % v/v PEG300, in presence of 1:50 ratio each of trypsin, alpha-chymotrypsin, pepsin, papain, proteinase K and subtilisin to MTHFD2 |
