3PGF
Crystal structure of maltose bound MBP with a conformationally specific synthetic antigen binder (sAB)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-D |
| Synchrotron site | APS |
| Beamline | 21-ID-D |
| Temperature [K] | 200 |
| Detector technology | CCD |
| Collection date | 2010-06-03 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.07817 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 63.870, 228.460, 135.570 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 38.070 - 2.100 |
| R-factor | 0.17903 |
| Rwork | 0.177 |
| R-free | 0.22664 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB ENTRIES 1ANF and 2R8S |
| RMSD bond length | 0.025 |
| RMSD bond angle | 1.954 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER (2.1.4) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.860 |
| High resolution limit [Å] | 1.830 | 4.970 | 1.830 |
| Rmerge | 0.060 | 0.029 | 0.516 |
| Number of reflections | 74893 | ||
| <I/σ(I)> | 12.2 | ||
| Completeness [%] | 85.2 | 98.3 | 39.7 |
| Redundancy | 4.5 | 4.7 | 2.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 292 | 19% PEG 3400, 8% Tacsimate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K |
