2WFO
Crystal structure of Machupo virus envelope glycoprotein GP1
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 51.523, 55.070, 61.327 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 32.070 - 1.730 |
| R-factor | 0.174 |
| Rwork | 0.172 |
| R-free | 0.21300 |
| Structure solution method | MAD |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.380 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | SHARP |
| Refinement software | REFMAC (5.5.0088) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.760 |
| High resolution limit [Å] | 1.730 | 1.730 |
| Rmerge | 0.110 | 0.710 |
| Number of reflections | 18458 | |
| <I/σ(I)> | 18.4 | 3.5 |
| Completeness [%] | 98.2 | 90.5 |
| Redundancy | 14.1 | 11.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.5 | 25% (W/V) PEG 3350, 0.2 M NACL, AND 0.1 M BIS-TRIS (PH 5.5) |
