3FVC
Crystal structure of a trimeric variant of the Epstein-Barr virus glycoprotein B
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 5ID-B |
| Synchrotron site | APS |
| Beamline | 5ID-B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-05-01 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 1.0379 |
| Spacegroup name | P 3 2 1 |
| Unit cell lengths | 106.800, 106.800, 210.750 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 26.610 - 3.200 |
| R-factor | 0.24635 |
| Rwork | 0.242 |
| R-free | 0.28292 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2gum |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.728 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | |
| High resolution limit [Å] | 3.200 | 3.200 |
| Number of reflections | 23367 | |
| <I/σ(I)> | 3 | |
| Completeness [%] | 98.5 | 91.6 |
| Redundancy | 8.3 | 4.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 10.5 | 298 | 0.1 M N-Cyclohexyl-3-aminopropanesulfonic acid (CAPS) pH 10.5 or 11.5, 1.40 M (NH4)2SO4 (AS) and 0.2 M Li2SO4, vapor diffusion, hanging drop, temperature 298K |
