1T0M
Conformational switch in polymorphic H-2K molecules containing an HSV peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RUH3R |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2003-01-29 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 66.310, 89.490, 89.260 |
Unit cell angles | 90.00, 111.46, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.000 |
R-factor | 0.233 |
Rwork | 0.233 |
R-free | 0.27100 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.006 |
RMSD bond angle | 1.310 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.059 | 0.356 |
Number of reflections | 45286 | |
<I/σ(I)> | 12.6 | 2.6 |
Completeness [%] | 69.9 | 44.3 |
Redundancy | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | PEG 8000, calcium acetate, sodium cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |