5V2I
Crystal structure of a mutant glycosylasparaginase (G172D) that causes the genetic disease Aspartylglucosaminuria
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X29A |
Synchrotron site | NSLS |
Beamline | X29A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-04-11 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9 |
Spacegroup name | P 1 |
Unit cell lengths | 46.040, 52.770, 61.890 |
Unit cell angles | 81.51, 90.15, 105.93 |
Refinement procedure
Resolution | 20.000 - 1.830 |
R-factor | 0.1577 |
Rwork | 0.156 |
R-free | 0.19667 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1p4k |
RMSD bond length | 0.020 |
RMSD bond angle | 1.915 |
Data reduction software | iMOSFLM |
Data scaling software | Aimless |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.150 | 1.870 |
High resolution limit [Å] | 1.830 | 1.830 |
Number of reflections | 45208 | |
<I/σ(I)> | 18.8 | |
Completeness [%] | 92.6 | |
Redundancy | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 298 | 0.2M Ammonium Acetate, 0.1M Bis-Tris pH 5.5, 25% Polyethylene glycol 3350 |