9CLD
Crystal structure of maltose binding protein (Apo)
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 | 2024-06-16 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.95372 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 43.819, 64.524, 57.640 |
| Unit cell angles | 90.00, 101.17, 90.00 |
Refinement procedure
| Resolution | 42.990 - 1.580 |
| R-factor | 0.1554 |
| Rwork | 0.154 |
| R-free | 0.17390 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.013 |
| 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] | 42.990 | 1.610 |
| High resolution limit [Å] | 1.580 | 1.580 |
| Number of reflections | 42986 | 2129 |
| <I/σ(I)> | 10.6 | 1.7 |
| Completeness [%] | 99.5 | |
| Redundancy | 5 | |
| CC(1/2) | 0.998 | 0.635 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 291.15 | 30% v/v PEG400, 100 mM sodium acetate (pH 4.6), 100 mM cadmium chloride |






