4KYC
Structure of the C-terminal domain of the Menangle virus phosphoprotein, fused to MBP.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-08-15 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9537 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 77.869, 77.869, 197.210 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 36.760 - 1.950 |
| R-factor | 0.18635 |
| Rwork | 0.185 |
| R-free | 0.21254 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB accession 1HSJ |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.384 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 36.760 | 1.980 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Number of reflections | 44924 | |
| <I/σ(I)> | 10.6 | 2.7 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 12.8 | 13.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 9.1 | 291.15 | 24 %(w/v) PEG8000, 0.2 M Boric acid/KOH, pH 9.1, VAPOR DIFFUSION, SITTING DROP, temperature 291.15K |
