1E0F
Crystal structure of the human alpha-thrombin-haemadin complex: an exosite II-binding inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH2R |
| Temperature [K] | 289 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-09-15 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 2 1 |
| Unit cell lengths | 121.670, 50.570, 129.740 |
| Unit cell angles | 90.00, 114.76, 90.00 |
Refinement procedure
| Resolution | 10.000 - 3.100 |
| R-factor | 0.208 |
| Rwork | 0.208 |
| R-free | 0.25500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4htc |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.520 * |
| Data reduction software | MOSFLM |
| Data scaling software | Agrovata |
| Phasing software | AMoRE |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 32.791 |
| High resolution limit [Å] | 3.100 |
| Rmerge | 0.109 |
| Total number of observations | 126754 * |
| Number of reflections | 23938 |
| Completeness [%] | 81.2 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 5.56 | 22 * | drop consists of equal amounts of protein and precipitant solutions * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 5 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 10 (mM) | |
| 3 | 1 | drop | 20 (mM) | ||
| 4 | 1 | drop | 0.02 (%(w/v)) | ||
| 5 | 1 | reservoir | sodium citrate | 100 (mM) | precipitant |
| 6 | 1 | reservoir | PEG4000 | 14 (%(w/v)) | precipitant |
| 7 | 1 | reservoir | isopropanol | 12.5 (%(v/v)) | precipitant |
