3NWF
Glycoprotein B from Herpes simplex virus type 1, low-pH
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CHESS BEAMLINE F1 |
| Synchrotron site | CHESS |
| Beamline | F1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-09-13 |
| Detector | ADSC QUANTUM 270 |
| Wavelength(s) | 0.9186 |
| Spacegroup name | P 3 |
| Unit cell lengths | 117.802, 117.802, 318.324 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 41.535 - 3.000 |
| R-factor | 0.1994 |
| Rwork | 0.197 |
| R-free | 0.24920 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3nwa |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.658 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.6.1_357)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.367 | 2.900 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.125 | |
| Number of reflections | 112550 | |
| <I/σ(I)> | 8.98 | 0.98 |
| Completeness [%] | 92.5 | 68 |
| Redundancy | 3.5 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 293 | 15% PEG 4000, 0.3M NaCl, and 0.1M sodium citrate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
