6PD4
Crystal Structure of Hendra Virus Attachment G Glycoprotein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-C |
| Synchrotron site | APS |
| Beamline | 24-ID-C |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2011-06-10 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 66.152, 73.244, 109.132 |
| Unit cell angles | 90.00, 91.85, 90.00 |
Refinement procedure
| Resolution | 36.924 - 2.200 |
| R-factor | 0.1687 |
| Rwork | 0.167 |
| R-free | 0.20700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.15.2_3472) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 40.000 | 40.000 | 2.280 |
| High resolution limit [Å] | 2.200 | 4.740 | 2.200 |
| Rmerge | 0.079 | 0.041 | 0.237 |
| Total number of observations | 169409 | ||
| Number of reflections | 51943 | 5456 | 4697 |
| <I/σ(I)> | 7.9 | ||
| Completeness [%] | 97.4 | 99.8 | 88.6 |
| Redundancy | 3.3 | 3.7 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 298 | 20% PEG2000MME and 130 mM (NH4)2SO4 |
