1YCP
THE CRYSTAL STRUCTURE OF FIBRINOGEN-AA PEPTIDE 1-23 (F8Y) BOUND TO BOVINE THROMBIN EXPLAINS WHY THE MUTATION OF PHE-8 TO TYROSINE STRONGLY INHIBITS NORMAL CLEAVAGE AT ARGININE-16
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 298 |
Detector technology | AREA DETECTOR |
Detector | SIEMENS |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 88.270, 88.270, 195.530 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 7.000 - 2.500 |
R-factor | 0.183 |
Rwork | 0.183 |
R-free | 0.24500 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.015 |
RMSD bond angle | 24.580 * |
Data reduction software | XENGEN |
Data scaling software | XENGEN |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 7.000 | |
High resolution limit [Å] | 2.350 | 2.500 * |
Rmerge | 0.109 | |
Number of reflections | 18614 | |
Completeness [%] | 63.0 | 25 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6 * | 2.0M AMMONIUM SULFATE 0.1M HEPES, PH 7.5 2.0% POLYETHYLENE GLYCOL 400 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | peptide | 15 (mg/ml) | |
2 | 1 | drop | ammonium phosphate | 0.25 (M) | |
3 | 1 | reservoir | ammonium sulfate | 2 (M) | |
4 | 1 | reservoir | HEPES | 0.1 (M) | |
5 | 1 | reservoir | PEG400 | 2 (%) |