1CJF
PROFILIN BINDS PROLINE-RICH LIGANDS IN TWO DISTINCT AMIDE BACKBONE ORIENTATIONS
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 298 |
Detector technology | AREA DETECTOR |
Collection date | 1998-07-01 |
Detector | SIEMENS X1000 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 105.400, 51.800, 77.500 |
Unit cell angles | 90.00, 131.10, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.300 |
Rwork | 0.195 |
R-free | 0.29300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1fil |
RMSD bond length | 0.009 |
RMSD bond angle | 28.070 * |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | X-PLOR |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 8.000 |
High resolution limit [Å] | 2.300 |
Rmerge | 0.052 |
Number of reflections | 11957 |
Completeness [%] | 90.0 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 | drop consists of equal volume of protein and reservoir solutions * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 8.5 (mg/ml) | |
2 | 1 | drop | peptide | 1:1.5 molar ratio | |
3 | 1 | reservoir | ammonium sulfate | 1.4 (M) | |
4 | 1 | reservoir | HEPES | 0.1 (M) | |
5 | 1 | reservoir | 0.1 (M) |