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 |