4W79
Crystal Structure of Human Protein N-terminal Glutamine Amidohydrolase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-D |
Synchrotron site | APS |
Beamline | 23-ID-D |
Detector technology | CCD |
Collection date | 2008-02-06 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97942 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 34.322, 64.039, 113.660 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 56.830 - 1.500 |
R-factor | 0.145 |
Rwork | 0.144 |
R-free | 0.16990 |
RMSD bond length | 0.017 |
RMSD bond angle | 1.913 |
Data scaling software | SCALEPACK |
Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 100.000 | 100.000 | 1.530 |
High resolution limit [Å] | 1.500 | 3.700 | 1.500 |
Rmerge | 0.105 | 0.058 | 0.543 |
Total number of observations | 498430 | ||
Number of reflections | 40943 | ||
<I/σ(I)> | 8.9 | ||
Completeness [%] | 99.5 | 99.5 | 95.9 |
Redundancy | 12.2 | 12.6 | 6.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 291 | PROTEIN SOLUTION (10 MG/ML SE-MET PROTEIN, 0.050 M SODIUM CHLORIDE, 0.003 M SODIUM AZIDE, 0.0003 M TCEP, BIS-TRIS PH 7.0) MIXED IN A 1:1 RATIO WITH THE WELL SOLUTION (1% ETHYLENE GLYCOL, 1.8 M AMMONIUM SULFATE, 0.10 M MES PH 6.0). CRYOPROTECTED IN FOUR STAGES WITH WELL SOLUTION USING 0 TO 25 % ETHYLENE GLYCOL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K |