1PUB
GM2-activator Protein crystal structure
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 298 |
| Detector technology | IMAGE PLATE |
| Collection date | 1995-02-20 |
| Detector | RIGAKU RAXIS |
| Wavelength(s) | 1.54041 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 40.070, 42.420, 113.780 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 7.990 - 2.510 |
| R-factor | 0.209 |
| Rwork | 0.209 |
| R-free | 0.28600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | monomer A of pdb entry 1G13 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.500 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.590 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.128 | 0.751 |
| Number of reflections | 7091 | |
| <I/σ(I)> | 3.5 | 1.3 |
| Completeness [%] | 98.6 | 98.7 |
| Redundancy | 3 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 298 | 21% Peg 4000, 0.1M acetate buffer, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
