3G26
Crystal structure of the C-terminal domain of the Rous Sarcoma Virus capsid protein: Mutant A184C
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX1 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.77337 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 32.243, 32.243, 113.993 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 27.920 - 1.550 |
| R-factor | 0.18796 |
| Rwork | 0.187 |
| R-free | 0.21365 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3g28 |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.611 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0044) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 28.000 | 1.610 |
| High resolution limit [Å] | 1.550 | 1.550 |
| Rmerge | 0.066 | 0.409 |
| Number of reflections | 10622 | |
| <I/σ(I)> | 8.1 | 1.2 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 10.5 | 10.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 3.7 | 291 | 0.1M Malic acid/KOH, pH3.7, 1.4 M Malonic acid/KOH, pH3.7, VAPOR DIFFUSION, SITTING DROP, temperature 291K |
