9PQP
Crystal structure of maltose binding protein (Apo), mutant Trp340 to 4-Fluorotryptophan
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2024-07-13 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.95366663 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 43.779, 64.643, 57.841 |
| Unit cell angles | 90.00, 101.50, 90.00 |
Refinement procedure
| Resolution | 42.620 - 1.070 |
| R-factor | 0.1388 |
| Rwork | 0.138 |
| R-free | 0.15740 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.978 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.21rc1_5058: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 42.900 | 1.090 |
| High resolution limit [Å] | 1.070 | 1.070 |
| Number of reflections | 134600 | 6002 |
| <I/σ(I)> | 16.9 | |
| Completeness [%] | 97.1 | 88.5 |
| Redundancy | 6.8 | |
| CC(1/2) | 1.000 | 0.556 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 298.5 | 30% v/v PEG400, 100 mM sodium acetate, pH 4.6, 100 mM cadmium chloride |
