8UA5
Crystal Structure of infected cell protein 0 (ICP0) from herpes simplex virus 1 (A636-Q776)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 17-ID |
| Synchrotron site | APS |
| Beamline | 17-ID |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-06-15 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 97.150, 97.150, 76.721 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 43.450 - 2.450 |
| R-factor | 0.1943 |
| Rwork | 0.192 |
| R-free | 0.25350 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.009 |
| RMSD bond angle | 0.991 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((dev_4336: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 43.450 | 2.550 |
| High resolution limit [Å] | 2.450 | 2.450 |
| Rmerge | 0.113 | 0.926 |
| Rmeas | 0.124 | 1.012 |
| Rpim | 0.048 | 0.402 |
| Total number of observations | 89786 | 9814 |
| Number of reflections | 14026 | 1562 |
| <I/σ(I)> | 13.1 | 1.6 |
| Completeness [%] | 99.9 | |
| Redundancy | 6.4 | 6.3 |
| CC(1/2) | 0.998 | 0.714 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 291 | PACT G3: 20% (w/v) PEG 3350, 100 mM Bis-Tris Propane pH 7.5, 200 mM NaI, 80% crystallization solution and 20% (v/v) PEG 200. |






