1FR3
THE HIGH RESOLUTION STRUCTURE OF A MOLYBDATE BINDING PROTEIN FROM SPOROMUSA OVATA
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X11 |
| Temperature [K] | 110 |
| Detector technology | IMAGE PLATE |
| Collection date | 1994-09-09 |
| Detector | MARRESEARCH |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 109.724, 138.328, 110.368 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.500 |
| Rwork | 0.185 |
| R-free | 0.19800 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.600 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.530 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.095 | 0.282 |
| Number of reflections | 129178 | |
| <I/σ(I)> | 4.2 | |
| Completeness [%] | 97.8 | 92.3 |
| Redundancy | 2.5 | 7.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 22 * | Wagner, U.G., (1994) J.Mol. Biol., 236, 388. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 5 (mg/ml) | |
| 2 | 1 | drop | PEG8000 | 15 (%(w/v)) | |
| 3 | 1 | drop | Tris-HCl | 0.05 (M) | |
| 4 | 1 | drop | 0.001 (mM) | ||
| 5 | 1 | drop | 0.001 (mM) | ||
| 6 | 1 | reservoir | PEG8000 | 30 (%(w/v)) | |
| 7 | 1 | reservoir | Tris-HCl | 0.1 (M) |
