2ID8
Crystal structure of Proteinase K
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 | 2006-03-31 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.98000 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 67.550, 67.550, 106.880 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.000 - 1.270 |
| R-factor | 0.1245 |
| R-free | 0.15880 |
| Structure solution method | AB INITIO PHASING |
| RMSD bond length | 0.014 |
| RMSD bond angle | 0.030 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | SHELXD |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 1.320 |
| High resolution limit [Å] | 1.270 | 1.270 |
| Rmerge | 0.033 | 0.131 |
| Number of reflections | 62172 | |
| <I/σ(I)> | 102.2 | 30.1 |
| Completeness [%] | 97.9 | 92.7 |
| Redundancy | 27.1 | 26.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 50 mg/ml protein, 0.5 M NaNO3, 50 mM citrate buffer, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
