6UP1
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 | 65.420, 75.250, 93.530 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 58.630 - 1.830 |
| R-factor | 0.2083 |
| Rwork | 0.205 |
| R-free | 0.26140 |
| Structure solution method | FOURIER SYNTHESIS |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.406 |
| 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] | 58.630 | 53.610 | 1.870 |
| High resolution limit [Å] | 1.830 | 8.970 | 1.830 |
| Rmerge | 0.101 | 0.058 | 0.479 |
| Rmeas | 0.113 | 0.065 | 0.530 |
| Rpim | 0.048 | 0.027 | 0.224 |
| Total number of observations | 2342 | 12491 | |
| Number of reflections | 41032 | 426 | 2471 |
| <I/σ(I)> | 9.7 | 17 | 2.8 |
| Completeness [%] | 99.1 | 99.6 | 97 |
| Redundancy | 5 | 5.5 | 5.1 |
| CC(1/2) | 0.992 | 0.988 | 0.887 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 283.15 | 0.1 M HEPES pH 7.5, 20% PEG 4000, and 10% 2-propanol |
