2E7V
Crystal structure of SEA domain of transmembrane protease from Mus musculus
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-11-15 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.9790, 0.9793, 0.9716 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 37.720, 42.740, 117.700 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 28.280 - 1.920 |
| R-factor | 0.191 |
| Rwork | 0.191 |
| R-free | 0.24100 |
| Structure solution method | MAD |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.300 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.000 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Number of reflections | 7162 | |
| <I/σ(I)> | 11.9 | 5.7 |
| Completeness [%] | 93.8 | 83.4 |
| Redundancy | 3.53 | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.3 | 293 | 45%(v/v) polypropylene glycol P 400, 0.1M Bis-Tris (pH 6.5), pH 6.3, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
