3F92
Crystal structure of ubiquitin-conjugating enzyme E2-25kDa (Huntington Interacting Protein 2) M172A mutant crystallized at pH 8.5
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-10-17 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.9700 |
| Spacegroup name | I 4 |
| Unit cell lengths | 134.817, 134.817, 38.211 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 42.640 - 2.230 |
| R-factor | 0.174 |
| Rwork | 0.172 |
| R-free | 0.21300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3e46 |
| RMSD bond length | 0.024 |
| RMSD bond angle | 1.850 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.310 |
| High resolution limit [Å] | 2.230 | 4.800 | 2.230 |
| Rmerge | 0.069 | 0.036 | 0.377 |
| Number of reflections | 16794 | ||
| <I/σ(I)> | 16.01 | ||
| Completeness [%] | 98.2 | 98.3 | 88.8 |
| Redundancy | 2.9 | 3 | 1.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 298 | Calcium acetate, Bicine, Tris-HCl, NaCl, PEG 400, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
