5H9C
Crystal structure of the ASLV fusion protein core
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CLSI BEAMLINE 08ID-1 |
Synchrotron site | CLSI |
Beamline | 08ID-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-02-22 |
Detector | RAYONIX MX-300 |
Wavelength(s) | 0.97949 |
Spacegroup name | H 3 |
Unit cell lengths | 42.800, 42.800, 119.428 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 39.809 - 1.783 |
R-factor | 0.1595 |
Rwork | 0.158 |
R-free | 0.19930 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4jpr |
RMSD bond length | 0.009 |
RMSD bond angle | 0.987 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 39.810 | 1.820 |
High resolution limit [Å] | 1.780 | 1.780 |
Rmerge | 0.060 | 0.708 |
Number of reflections | 7712 | |
<I/σ(I)> | 17.38 | 1.7 |
Completeness [%] | 98.9 | 80.2 |
Redundancy | 5.5 | 2.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 295 | 20% (w/v) 2-methyl-2,4-pentanediol, 5% (w/v) PEG 8000, and 0.1 M sodium cacodylate |