6UPF
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 | 2019-07-05 |
| Detector | DECTRIS PILATUS 2M |
| Wavelength(s) | 1.4586 |
| Spacegroup name | P 2 21 21 |
| Unit cell lengths | 47.830, 75.160, 151.920 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 75.960 - 1.650 |
| R-factor | 0.1646 |
| Rwork | 0.163 |
| R-free | 0.19700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4poc |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.953 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless (0.5.32) |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 75.960 | 45.620 | 1.680 |
| High resolution limit [Å] | 1.650 | 9.030 | 1.650 |
| Rmerge | 0.084 | 0.038 | 0.714 |
| Rmeas | 0.099 | 0.044 | 0.845 |
| Rpim | 0.052 | 0.022 | 0.442 |
| Total number of observations | 1692 | 10926 | |
| Number of reflections | 66128 | 469 | 3208 |
| <I/σ(I)> | 8.5 | 20.6 | 1.8 |
| Completeness [%] | 99.0 | 95.7 | 99.4 |
| Redundancy | 3.4 | 3.6 | 3.4 |
| CC(1/2) | 0.995 | 0.997 | 0.523 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 283 | 0.05 M Tris-HCl pH 7.5, 0.05 M NaCl, 1 mM EDTA, 15% PEG 4000 and 2 mM 2-PG |
