6UP8
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 | 2018-11-15 |
| Detector | DECTRIS PILATUS 2M |
| Wavelength(s) | 1.4586 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 64.960, 74.830, 92.820 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 58.260 - 2.000 |
| R-factor | 0.1979 |
| Rwork | 0.195 |
| R-free | 0.25280 |
| Structure solution method | FOURIER SYNTHESIS |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.407 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless (0.5.32) |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 64.960 | 64.960 | 2.050 |
| High resolution limit [Å] | 2.000 | 8.940 | 2.000 |
| Rmerge | 0.095 | 0.030 | 0.554 |
| Rmeas | 0.106 | 0.034 | 0.627 |
| Rpim | 0.047 | 0.015 | 0.288 |
| Total number of observations | 151264 | 2135 | 9761 |
| Number of reflections | 31078 | 423 | 2211 |
| <I/σ(I)> | 9.3 | 21.6 | 2 |
| Completeness [%] | 99.4 | 99.7 | 97.8 |
| Redundancy | 4.9 | 5 | 4.4 |
| CC(1/2) | 0.996 | 0.995 | 0.859 |
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 |
