2D26
Active site distortion is sufficient for proteinase inhibit second crystal structure of covalent serpin-proteinase complex
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 | 2004-12-18 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 1.0 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 109.830, 85.180, 76.260 |
Unit cell angles | 90.00, 121.01, 90.00 |
Refinement procedure
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 3.450 |
High resolution limit [Å] | 3.300 | 3.300 |
Rmerge | 0.078 | 0.275 |
Number of reflections | 8959 | |
<I/σ(I)> | 9.5 | 5.7 |
Completeness [%] | 97.8 | 96.4 |
Redundancy | 3.6 | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.1 | 291 | PEG3350, pH 8.10, VAPOR DIFFUSION, HANGING DROP, temperature 291K |