3IOQ
Crystal structure of the Carica candamarcensis cysteine protease CMS1MS2 in complex with E-64.
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 | 2008-10-07 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 1.458 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 73.639, 73.639, 118.786 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 62.600 - 1.870 |
| R-factor | 0.164 |
| Rwork | 0.162 |
| R-free | 0.19300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Model predicted by SwissModel using the primary structure of CMS1MS2 and the structures of caricain (PDBID 1MEG) chymopapain (PDBID 1YAL) and papain (PDBID 1PPN) |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.301 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 62.600 | 1.930 |
| High resolution limit [Å] | 1.870 | 1.870 |
| Rmerge | 0.081 | 0.251 |
| Number of reflections | 27792 | |
| <I/σ(I)> | 45.8 | 17 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 28.1 | 27.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 291 | 0.2 M ammonium sulfate, 25% PEG 4000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
