4ICK
Crystal structure of human AP4A hydrolase E58A mutant
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL17U |
| Synchrotron site | SSRF |
| Beamline | BL17U |
| Collection date | 2012-05-26 |
| Wavelength(s) | 1.00584 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 72.190, 72.190, 133.510 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.100 |
| R-factor | 0.1889 |
| Rwork | 0.186 |
| R-free | 0.23464 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3u53 |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.589 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.154 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Number of reflections | 20197 | |
| Completeness [%] | 100.0 | 99.77 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.4 | 285 | 0.1M Tris (pH 8.4), 2.0M Ammonium phosphate monobasic, 5mM magnesium chloride, temperature 285K, VAPOR DIFFUSION, HANGING DROP |
