1W94
Crystal Structure of Mil (Mth680), an archaeal Imp4-like protein
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-06-26 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.97935, 0.9795, 0.976565 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 33.673, 77.533, 60.965 |
| Unit cell angles | 90.00, 100.01, 90.00 |
Refinement procedure
| Resolution | 60.080 - 2.000 |
| R-factor | 0.2 |
| Rwork | 0.198 |
| R-free | 0.24000 |
| Structure solution method | MAD |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.401 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | SHELX |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.460 | 2.020 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.110 | 0.570 |
| Number of reflections | 20938 | |
| <I/σ(I)> | 9.23 | 1.47 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 3.9 | 3.87 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | THE PROTEIN AT APPROX. 10 MG/ML WAS CRYSTALLIZED IN 20% PEG3350 AND 0.1 M HEPES 7.5, pH 7.50 |
