3SJE
X-ray structure of human glutamate carboxypeptidase II (the E424A inactive mutant) in complex with N-acetyl-aspartyl-aminononanoic acid
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-01-11 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 1.00 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 101.824, 130.231, 159.171 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.570 - 1.700 |
R-factor | 0.17338 |
Rwork | 0.173 |
R-free | 0.18809 |
Structure solution method | FOURIER SYNTHESIS |
RMSD bond length | 0.020 |
RMSD bond angle | 1.736 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | REFMAC |
Refinement software | REFMAC |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 30.000 |
High resolution limit [Å] | 1.700 |
Rmerge | 0.080 |
Number of reflections | 111992 |
<I/σ(I)> | 20.8 |
Completeness [%] | 96.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | 33% (v/v) pentaerythritol propoxylate PO/OH 5/4, 0.5 % (w/v) PEG 3350, 100 mM Tris-HCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |