6RS1
Dipeptide Gly-Pro binds to a glycolytic enzyme fructose bisphosphate aldolase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-06-24 |
| Detector | DECTRIS PILATUS 6M-F |
| Wavelength(s) | 1.072 |
| Spacegroup name | P 1 |
| Unit cell lengths | 67.567, 67.636, 88.908 |
| Unit cell angles | 79.95, 73.13, 65.58 |
Refinement procedure
| Resolution | 48.370 - 1.900 |
| R-factor | 0.21631 |
| Rwork | 0.214 |
| R-free | 0.25381 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5ky6 |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.566 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0230) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.370 | 2.040 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.178 | 1.194 |
| Rmeas | 0.200 | 1.340 |
| Rpim | 0.090 | 0.600 |
| Number of reflections | 88957 | 4572 |
| <I/σ(I)> | 7.04 | |
| Completeness [%] | 83.5 | |
| Redundancy | 4.9 | |
| CC(1/2) | 0.992 | 0.623 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.2 M Lithium Sulfate, 0.1 M Bis-Tris pH 6.2 and 25% PEG 3350 |
