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 |