3QJ3
Structure of digestive procathepsin L2 proteinase from Tenebrio molitor larval midgut
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | LNLS BEAMLINE W01B-MX2 |
Synchrotron site | LNLS |
Beamline | W01B-MX2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-03-30 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 1.46 |
Spacegroup name | P 1 |
Unit cell lengths | 51.669, 52.370, 59.716 |
Unit cell angles | 91.28, 91.55, 109.59 |
Refinement procedure
Resolution | 34.560 - 1.850 |
R-factor | 0.1856 |
Rwork | 0.183 |
R-free | 0.23149 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3qt4 |
RMSD bond length | 0.009 |
RMSD bond angle | 1.081 |
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] | 42.000 | 1.920 |
High resolution limit [Å] | 1.850 | 1.850 |
Rmerge | 0.054 | 0.318 |
Number of reflections | 44108 | |
<I/σ(I)> | 18.2 | 2.5 |
Completeness [%] | 87.7 | 10 |
Redundancy | 3.8 | 2.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.7 | 289 | pCAL2Cys25Ser (10 mg/ml), 0.2 M sodium acetate, 0.1 M sodium cacodylate, 20% PEG 8000, pH 6.7, VAPOR DIFFUSION, SITTING DROP, temperature 289K |