1C5M
STRUCTURAL BASIS FOR SELECTIVITY OF A SMALL MOLECULE, S1-BINDING, SUB-MICROMOLAR INHIBITOR OF UROKINASE TYPE PLASMINOGEN ACTIVATOR
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Temperature [K] | 298 |
| Detector technology | IMAGE PLATE |
| Collection date | 1999-03-04 |
| Detector | RIGAKU RAXIS IV++ |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 81.820, 81.820, 108.790 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 7.500 - 1.950 |
| R-factor | 0.226 * |
| Rwork | 0.218 |
| R-free | 0.30700 |
| Starting model (for MR) | 1fxa |
| RMSD bond length | 0.017 * |
| RMSD bond angle | 3.900 |
| Data reduction software | bioteX ((MSC)) |
| Data scaling software | bioteX |
| Phasing software | X-PLOR (3.1) |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 70.860 | 2.040 |
| High resolution limit [Å] | 1.640 | 1.950 |
| Rmerge | 0.072 | 0.265 |
| <I/σ(I)> | 6.5 | 1.6 |
| Completeness [%] | 60.0 | 32.2 |
| Redundancy | 1.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 | crystallization conditions : Crystals of truncated human factor Xa were grown in hanging drops from equal volumes of protein solution (5.0 mg/ml in 20 mM Hepes, 50 mM ammonimum sulfate, pH 8.0) and well solution (25 % PEG 5K, 0.10 M Hepes, 0.2 M ammonium sulfate, pH 7.5)., VAPOR DIFFUSION |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 5.0 (mg/ml) | |
| 2 | 1 | drop | HEPES | 20 (mM) | |
| 3 | 1 | drop | ammonium sulfate | 50 (mM) | |
| 4 | 1 | reservoir | PEG5000 | 25 (%) | |
| 5 | 1 | reservoir | HEPES | 0.10 (M) | |
| 6 | 1 | reservoir | ammonium sulfate | 0.2 (M) |
