1PU5
GM2-activator Protein crystal structure
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 17-BM |
| Synchrotron site | APS |
| Beamline | 17-BM |
| Temperature [K] | 123 |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 63.320, 86.130, 120.210 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 7.990 - 1.900 |
| R-factor | 0.214 |
| Rwork | 0.214 |
| R-free | 0.25300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1g13 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.600 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.970 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.049 | 0.515 |
| Number of reflections | 50312 | |
| <I/σ(I)> | 5 | |
| Completeness [%] | 97.2 | |
| Redundancy | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.7 | 278 | Peg 4000, iso-propanol, Hepes buffer, pH 7.7, VAPOR DIFFUSION, HANGING DROP, temperature 278.0K |






