6UP5
Triosephosphate isomerase deficiency: Effect of F240L mutation on enzyme structure
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | LNLS BEAMLINE W01B-MX2 |
| Synchrotron site | LNLS |
| Beamline | W01B-MX2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-07-03 |
| Detector | DECTRIS PILATUS 2M |
| Wavelength(s) | 1.4586 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 65.380, 74.570, 92.870 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 58.150 - 1.920 |
| R-factor | 0.1839 |
| Rwork | 0.181 |
| R-free | 0.23220 |
| Structure solution method | FOURIER SYNTHESIS |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.367 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 58.150 | 58.150 | 1.970 |
| High resolution limit [Å] | 1.920 | 9.020 | 1.920 |
| Rmerge | 0.056 | 0.043 | 0.151 |
| Rmeas | 0.068 | 0.053 | 0.184 |
| Rpim | 0.038 | 0.029 | 0.102 |
| Total number of observations | 97605 | 1155 | 6561 |
| Number of reflections | 34287 | 381 | 2247 |
| <I/σ(I)> | 12.7 | 18.7 | 5.8 |
| Completeness [%] | 97.6 | 95.3 | 97.4 |
| Redundancy | 2.8 | 3 | 2.9 |
| CC(1/2) | 0.995 | 0.993 | 0.962 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 283 | 0.1 M HEPES pH 7.5, 20% PEG 4000, and 10% 2-propanol |
