2P82
Cysteine protease ATG4A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-D |
Synchrotron site | APS |
Beamline | 23-ID-D |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-02-22 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 1.00000 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 94.408, 94.408, 337.339 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 38.690 - 2.100 |
R-factor | 0.17679 |
Rwork | 0.175 |
R-free | 0.21279 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1dli |
RMSD bond length | 0.011 |
RMSD bond angle | 1.150 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 39.000 | 2.180 |
High resolution limit [Å] | 2.100 | 2.100 |
Number of reflections | 98033 | |
<I/σ(I)> | 31.86 | 2.7 |
Completeness [%] | 95.2 | 68.1 |
Redundancy | 7.6 | 5.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.4 | 291 | Protein concentration 10 mg/mL. Reservoir: 23.5% PEG3350, 0.2M NaCl, 0.1M SPG buffer pH 5.4, 5% ethylene glycol. Cryoprotected in 20% ethylene glycol, VAPOR DIFFUSION, HANGING DROP, temperature 291.0K |