1IZ2
Interactions causing the kinetic trap in serpin protein folding
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PAL/PLS BEAMLINE 6B |
Synchrotron site | PAL/PLS |
Beamline | 6B |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2001-06-20 |
Detector | MACSCIENCE |
Wavelength(s) | 1.1 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 63.020, 74.173, 93.115 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 * - 2.200 |
R-factor | 0.221 |
Rwork | 0.211 |
R-free | 0.27900 * |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 * |
RMSD bond angle | 1.333 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 * | |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.059 * | 0.253 * |
Number of reflections | 21991 * | 2115 * |
Completeness [%] | 96.6 * | 94.3 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.6 * | 22 * | Ammonium Sulfate 1.8M, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | ammonium sulfate | 1.8 (M) | |
2 | 1 | drop | sodium potassium tartrate | 0.2 (M) | |
3 | 1 | drop | sodium citrate | 0.1 (M) | pH5.6 |
4 | 1 | drop | n-octanol-sucrose | 5 (%) | |
5 | 1 | drop | protein | 12 (mg/ml) |