1ND5
Crystal Structures of Human Prostatic Acid Phosphatase in Complex with a Phosphate Ion and alpha-Benzylaminobenzylphosphonic Acid Update the Mechanistic Picture and Offer New Insights into Inhibitor Design
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 298 |
| Detector technology | IMAGE PLATE |
| Collection date | 1997-12-01 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 120.100, 204.860, 71.220 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 * - 2.900 |
| R-factor | 0.2051 |
| Rwork | 0.205 |
| R-free | 0.27800 * |
| Structure solution method | FOURIER SYNTHESIS |
| Starting model (for MR) | 2hpa |
| RMSD bond length | 0.007 * |
| RMSD bond angle | 1.300 * |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 3.000 |
| High resolution limit [Å] | 2.900 * | 2.890 |
| Rmerge | 0.063 | |
| Number of reflections | 33191 | |
| Completeness [%] | 82.2 | 63.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | unknown * | 10 | 298 | PEG, KCL, Glycine, pH 10.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | protein | 7-10 (mg/ml) | |
| 2 | 1 | 1 | PEG1500 | 30 (%) | |
| 3 | 1 | 1 | PEG1000 | 7 (%) | |
| 4 | 1 | 1 | PEG400 | 6 (%) | |
| 5 | 1 | 1 | 100 (mM) | ||
| 6 | 1 | 1 | glycine | 100 (mM) | pH10.0 |
