9E97
L-allo-threonine aldolase from Thermotoga maritima N308E-Y87A-R122G-P121D Mutant with a 2-(aminomethyl)pyridine PLP modification
This is a non-PDB format compatible entry.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS-II BEAMLINE 17-ID-1 |
| Synchrotron site | NSLS-II |
| Beamline | 17-ID-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2024-09-15 |
| Detector | DECTRIS EIGER X 9M |
| Wavelength(s) | 0.92015 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 94.208, 166.022, 93.978 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.560 - 1.530 |
| R-factor | 0.1702 |
| Rwork | 0.169 |
| R-free | 0.18560 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.853 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.17_3644) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.560 | 1.570 |
| High resolution limit [Å] | 1.530 | 1.530 |
| Rmerge | 0.067 | 0.702 |
| Rmeas | 0.072 | 0.772 |
| Rpim | 0.028 | 0.317 |
| Total number of observations | 45592 | |
| Number of reflections | 109793 | 7905 |
| <I/σ(I)> | 19.2 | 2.3 |
| Completeness [%] | 99.8 | |
| Redundancy | 6.8 | 5.8 |
| CC(1/2) | 1.000 | 0.769 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.2 | 293 | HEPES buffer pH 7.2, calcium acetate, PEG 400 |
