1CR9
CRYSTAL STRUCTURE OF THE ANTI-PRION FAB 3F4
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 298 |
Detector technology | IMAGE PLATE |
Collection date | 1996-10-30 |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 98.900, 77.600, 70.600 |
Unit cell angles | 90.00, 110.56, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.000 |
R-factor | 0.171 * |
Rwork | 0.171 |
R-free | 0.21700 |
RMSD bond length | 0.011 |
RMSD bond angle | 1.782 |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.050 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.055 | 0.220 |
Number of reflections | 33314 * | 2242 * |
<I/σ(I)> | 10.1 | |
Completeness [%] | 98.5 | 90.6 |
Redundancy | 3.4 | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 * | 298 | ammonium sulphate, PEG 400, HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | MOPS | 10 (mM) | |
2 | 1 | drop | protein | 20 (mg/ml) | |
3 | 1 | drop | 50 (mM) | ||
4 | 1 | drop | 2 (mM) | ||
5 | 1 | reservoir | ammonium sulfate | 2.0 (M) | |
6 | 1 | reservoir | PEG400 | 2 (%(v/v)) | |
7 | 1 | reservoir | HEPES | 100 (mM) |