1IEF
CRYSTAL STRUCTURE OF THE CATALYTIC SITE MUTANT S134A OF THE HUMAN CYTOMEGALOVIRUS PROTEASE
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 32-ID |
| Synchrotron site | APS |
| Beamline | 32-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2000-11-20 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 76.400, 76.400, 171.800 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.340 - 2.300 |
| R-factor | 0.229 |
| Rwork | 0.229 |
| R-free | 0.27000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.200 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | GLRF |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.380 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.070 | 0.154 |
| Total number of observations | 108421 * | |
| Number of reflections | 23000 | |
| <I/σ(I)> | 23.73 | |
| Completeness [%] | 98.6 | 96.4 |
| Redundancy | 6.05 | 3.92 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5 * | 21 * | 20% PEG3350, 0.1M MES 6.0, 15% GLYCEROL, 5% t-BuOH, 0.3M NaCl, VAPOR DIFFUSION, HANGING DROP, temperature 294K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 14 (mg/ml) | |
| 2 | 1 | drop | 20 (mM) | ||
| 3 | 1 | drop | 80 (mM) | ||
| 4 | 1 | reservoir | PEG3350 | 19-21 (%) | |
| 5 | 1 | reservoir | MES | 0.1 (M) | |
| 6 | 1 | reservoir | glycerol | 15 (%) | |
| 7 | 1 | reservoir | tert-butyl alcohol | 5 (%) | |
| 8 | 1 | reservoir | 0.3-0.4 (M) |
