2GHW
Crystal structure of SARS spike protein receptor binding domain in complex with a neutralizing antibody, 80R
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.3 |
| Synchrotron site | ALS |
| Beamline | 5.0.3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-09-20 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.11587 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 47.453, 175.902, 67.561 |
| Unit cell angles | 90.00, 96.55, 90.00 |
Refinement procedure
| Resolution | 45.550 - 2.300 |
| R-factor | 0.25085 |
| Rwork | 0.248 |
| R-free | 0.29537 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2AJF CHAIN F 1DZB CHAIN A |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.217 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.380 |
| High resolution limit [Å] | 2.290 | 2.290 |
| Rmerge | 0.145 | 0.571 |
| Number of reflections | 51915 | |
| <I/σ(I)> | 8.8 | 1.9 |
| Completeness [%] | 93.8 | 87 |
| Redundancy | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 290 | 12.5% PEG4000, 0.1M sodium acetate, 0.2M ammonium sulfate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 290K |
