3RLF
Crystal structure of the maltose-binding protein/maltose transporter complex in an outward-facing conformation bound to MgAMPPNP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-08-05 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.03320 |
| Spacegroup name | P 1 |
| Unit cell lengths | 72.098, 95.812, 109.983 |
| Unit cell angles | 86.70, 82.68, 76.40 |
Refinement procedure
| Resolution | 20.000 - 2.200 |
| R-factor | 0.22481 |
| Rwork | 0.223 |
| R-free | 0.25406 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2r6g |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.012 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.320 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.054 | |
| Number of reflections | 127961 | |
| <I/σ(I)> | 1.6 | 2 |
| Completeness [%] | 88.1 | 56.7 |
| Redundancy | 2 | 1.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 28% PEG 4000, 0.1M sodium hepes pH 7.5, 0.2M sodium chloride, 0.05M magnesium chloride, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
