2IPH
X-ray Structure at 1.75 A Resolution of a Norovirus Protease Linked to an Active Site Directed Peptide Inhibitor
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Detector technology | CCD |
| Collection date | 2004-04-05 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.97625,0.97925,0.97955 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 49.497, 84.106, 121.471 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.400 - 1.750 |
| Rwork | 0.204 |
| R-free | 0.22100 |
| Structure solution method | MAD |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | SOLVE (2.08) |
| Refinement software | CNS |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 36.491 | 40.490 | 1.790 |
| High resolution limit [Å] | 1.700 | 5.380 | 1.700 |
| Rmerge | 0.053 | 0.032 | 0.623 |
| Total number of observations | 11332 | 38859 | |
| Number of reflections | 55934 | ||
| <I/σ(I)> | 8.9 | 19 | 1.2 |
| Completeness [%] | 98.8 | 97.3 | 92.8 |
| Redundancy | 6.7 | 5.9 | 5.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | ||||
| 1 | ||||
| 1 |
