3U82
Binding of herpes simplex virus glycoprotein D to nectin-1 exploits host cell adhesion
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL17U |
| Synchrotron site | SSRF |
| Beamline | BL17U |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-07-19 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97916 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 52.532, 169.043, 183.316 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 38.378 - 3.164 |
| R-factor | 0.3223 |
| Rwork | 0.321 |
| R-free | 0.34430 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2c36 3alp |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.343 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.5_2)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 3.310 |
| High resolution limit [Å] | 3.164 | 3.200 |
| Rmerge | 0.102 | 0.504 |
| Number of reflections | 13572 | |
| <I/σ(I)> | 14.4 | 1.7 |
| Completeness [%] | 94.9 | 82.7 |
| Redundancy | 4.2 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 277 | 20% PEG 1000, 0.1M lithium sulfate monohydrate, 0.1M sodium citrate tribasic dehydrate, pH 5.5 , VAPOR DIFFUSION, HANGING DROP, temperature 277K |
