2VK2
Crystal structure of a galactofuranose binding protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-10-05 |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 45.745, 51.535, 116.091 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.200 |
| R-factor | 0.179 |
| Rwork | 0.178 |
| R-free | 0.19000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1dbp |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.206 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.240 |
| High resolution limit [Å] | 1.200 | 1.200 |
| Rmerge | 0.070 | 0.350 |
| Number of reflections | 78867 | |
| <I/σ(I)> | 22 | 1.5 |
| Completeness [%] | 91.0 | 39 |
| Redundancy | 6.1 | 1.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6 | MALIC, MES, TRIS, BUFFER SYSTEM PH 6; 25% PEG 1.5K |
