1G0V
THE STRUCTURE OF PROTEINASE A COMPLEXED WITH A IA3 MUTANT, MVV
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X9B |
| Synchrotron site | NSLS |
| Beamline | X9B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1999-07-08 |
| Detector | ADSC QUANTUM 4 |
| Spacegroup name | P 62 2 2 |
| Unit cell lengths | 191.140, 191.140, 52.334 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 24.410 - 2.000 |
| R-factor | 0.198 |
| Rwork | 0.198 |
| R-free | 0.23100 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 25.400 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.970 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.087 | 0.346 |
| Total number of observations | 217446 * | |
| Number of reflections | 41718 | |
| <I/σ(I)> | 12.7 | |
| Completeness [%] | 92.8 | 75.5 |
| Redundancy | 5.2 | 1.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 6 * | 298 | PEG 1500, (NH4)2SO4, pH 5.6, VAPOR DIFFUSION, HANGING DROP at 298K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 5 (mg/ml) | |
| 2 | 1 | reservoir | PEG1500 | 30 (%) | |
| 3 | 1 | reservoir | ammonium sulfate | 0.14 (M) | |
| 4 | 1 | reservoir | MES | 0.1 (M) |
