1TD0
Viral capsid protein SHP at pH 5.5
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 100 |
Wavelength(s) | 1.54 |
Spacegroup name | P 3 |
Unit cell lengths | 57.482, 57.482, 101.608 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 28.740 - 1.950 |
R-factor | 0.229 |
Rwork | 0.229 |
R-free | 0.26000 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.006 |
RMSD bond angle | 1.200 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.020 |
High resolution limit [Å] | 1.950 | 1.950 |
Rmerge | 0.076 | 0.514 |
Number of reflections | 27034 | |
<I/σ(I)> | 2.6 | |
Completeness [%] | 98.5 | 98.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 295 | sodium Acetate, PEG 5000 MME, MgCl2, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |