3NWA
Glycoprotein B from Herpes simplex virus type 1, W174R mutant, low-pH
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X25 |
| Synchrotron site | NSLS |
| Beamline | X25 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-11-12 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9795 |
| Spacegroup name | P 3 |
| Unit cell lengths | 117.090, 117.090, 321.378 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 47.316 - 2.263 |
| R-factor | 0.1757 |
| Rwork | 0.172 |
| R-free | 0.22700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2gum |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.004 |
| 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] | 48.352 | 2.300 |
| High resolution limit [Å] | 2.263 | 2.260 |
| Rmerge | 0.120 | |
| Number of reflections | 227148 | |
| <I/σ(I)> | 7.57 | 1.06 |
| Completeness [%] | 98.8 | 72 |
| Redundancy | 2.3 | 1.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 293 | 7% PEG 4000, 0.5M NaCl, 0.1M sodium citrate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
