7T0Q
human triosephosphate isomerase mutant v154m
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 21 21 21 |
| Unit cell lengths | 65.010, 75.430, 91.830 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 58.290 - 2.000 |
| R-factor | 0.1516 |
| Rwork | 0.149 |
| R-free | 0.20650 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6up1 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.417 |
| 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] | 65.010 | 65.010 | 2.050 |
| High resolution limit [Å] | 2.000 | 8.940 | 2.000 |
| Rmerge | 0.100 | 0.021 | 0.534 |
| Rmeas | 0.110 | 0.023 | 0.594 |
| Rpim | 0.046 | 0.010 | 0.254 |
| Total number of observations | 164877 | 2363 | 10187 |
| Number of reflections | 30218 | 423 | 2005 |
| <I/σ(I)> | 12.2 | 31.4 | 2.8 |
| Completeness [%] | 96.9 | 99.9 | 88.6 |
| Redundancy | 5.5 | 5.6 | 5.1 |
| CC(1/2) | 0.997 | 0.998 | 0.861 |
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 |
