1S1D
Structure and protein design of human apyrase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X4A |
| Synchrotron site | NSLS |
| Beamline | X4A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-06-01 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.98 |
| Spacegroup name | P 1 |
| Unit cell lengths | 43.163, 52.450, 77.478 |
| Unit cell angles | 98.99, 106.99, 100.09 |
Refinement procedure
| Resolution | 46.600 - 1.600 |
| R-factor | 0.16581 |
| Rwork | 0.164 |
| R-free | 0.19400 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1s18 |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.500 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.600 | 1.660 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.059 | 0.348 |
| Number of reflections | 79084 | |
| <I/σ(I)> | 12 | 2.3 |
| Completeness [%] | 95.0 | 93.8 |
| Redundancy | 1.9 | 1.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5 | 295 | PEG MME 2000, sodium acetate, ammonium sulfate, strontium chloride, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | PEG2000 MME | 10-15 (%) | |
| 2 | 1 | reservoir | 100 (mM) | pH5.0 | |
| 3 | 1 | reservoir | ammonium sulfate | 0.3-0.4 (M) | |
| 4 | 1 | drop | protein | 15 (mg/ml) |
