3M88
Crystal structure of the cysteine protease inhibitor, EhICP2, from Entamoeba histolytica
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-D |
| Synchrotron site | APS |
| Beamline | 21-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-11-06 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.078 |
| Spacegroup name | P 2 21 21 |
| Unit cell lengths | 59.041, 60.507, 60.660 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.253 - 1.900 |
| R-factor | 0.188 |
| Rwork | 0.185 |
| R-free | 0.22800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2nnr |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.107 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (3.3.9) |
| Phasing software | PHASER (2.1.4) |
| Refinement software | PHENIX (1.6_289) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.253 | 2.000 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.137 | 0.732 |
| Number of reflections | 17712 | |
| <I/σ(I)> | 11.8 | 5.4 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 9.5 | 9.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 294.15 | 0.2M Ammonium sulfate; 30% PEG 8000; 0.1M Sodium cacodylate, pH 6.5, vapor diffusion, hanging drop, temperature 294.15K |
