1EB2
Trypsin inhibitor complex (BPO)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX7.2 |
Synchrotron site | SRS |
Beamline | PX7.2 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 60.080, 63.825, 70.040 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.000 - 2.000 |
R-factor | 0.178 |
Rwork | 0.178 |
R-free | 0.24400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3ptn |
RMSD bond length | 0.009 |
RMSD bond angle | 1.800 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.0) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 30.000 |
High resolution limit [Å] | 2.000 |
Rmerge | 0.059 |
Number of reflections | 17272 |
Completeness [%] | 91.6 |
Redundancy | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 8 * | 2.1 M AMMONIUM SULPHATE, 0.05 M TRIS PH 8.15 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 15 (mg/ml) | |
2 | 1 | drop | Tris | 0.05 (M) | pH8. |
3 | 1 | drop | 3 (mM) | ||
4 | 1 | drop | acetonitrile | 18 (%) | |
5 | 1 | drop | DMF | 5 (%) | |
6 | 1 | reservoir | ammonium sulfate | 2.1 (M) | |
7 | 1 | reservoir | Tris | 0.05 (M) | pH8.15 |