7R70
Crystal Structure of the UbArk2C fusion protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX1 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2018-03-09 |
| Detector | ADSC QUANTUM 210r |
| Wavelength(s) | 0.9537 |
| Spacegroup name | P 62 2 2 |
| Unit cell lengths | 154.470, 154.470, 81.706 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 44.590 - 2.499 |
| R-factor | 0.202 |
| Rwork | 0.200 |
| R-free | 0.24460 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5d0k |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.883 |
| Data reduction software | XDS (20190315) |
| Data scaling software | Aimless (0.6.2) |
| Phasing software | PHASER (2.8.2) |
| Refinement software | PHENIX (1.13_2998) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 44.592 | 44.590 | 2.590 |
| High resolution limit [Å] | 2.490 | 8.990 | 2.490 |
| Rmerge | 0.193 | 0.035 | 3.190 |
| Rmeas | 0.196 | 0.036 | 3.228 |
| Rpim | 0.030 | 0.006 | 0.490 |
| Total number of observations | 16789 | 89409 | |
| Number of reflections | 20455 | 524 | 2141 |
| <I/σ(I)> | 22.6 | 91.7 | 1.6 |
| Completeness [%] | 99.4 | 99.3 | 95.2 |
| Redundancy | 42.8 | 32 | 41.8 |
| CC(1/2) | 0.999 | 1.000 | 0.602 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 289.15 | 1.6 M tri-sodium citrate |
