9XPU
Maltose-binding protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL26B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL26B1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2024-07-19 |
| Detector | DECTRIS EIGER R 4M |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 70.421, 64.448, 82.399 |
| Unit cell angles | 90.00, 96.94, 90.00 |
Refinement procedure
| Resolution | 28.010 - 1.500 |
| R-factor | 0.1932 |
| Rwork | 0.192 |
| R-free | 0.22500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | AlphaFold |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.818 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((1.21.1_5286: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.380 | 1.530 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmeas | 0.037 | 0.803 |
| Rpim | 0.023 | 0.520 |
| Number of reflections | 116395 | 5405 |
| <I/σ(I)> | 21.5 | 2.5 |
| Completeness [%] | 99.2 | |
| Redundancy | 6.7 | |
| CC(1/2) | 1.000 | 0.775 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 7.5 | 293 | 1.4 M sodium citrate |
