2CFI
The hydrolase domain of human 10-FTHFD in complex with 6- formyltetrahydropterin
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.1 |
| Synchrotron site | BESSY |
| Beamline | 14.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | MARRESEARCH |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 108.140, 64.440, 58.870 |
| Unit cell angles | 90.00, 98.79, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.850 |
| R-factor | 0.181 |
| Rwork | 0.178 |
| R-free | 0.22500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2bw0 |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.575 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.900 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.070 | 0.410 |
| Number of reflections | 34108 | |
| <I/σ(I)> | 14.3 | 4 |
| Completeness [%] | 99.6 | 99.5 |
| Redundancy | 4.8 | 4.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.8 | 1.4 M AMMONIUM SULFATE, 50 MM HEPES PH 7.8 |
