1E32
Structure of the N-Terminal domain and the D1 AAA domain of membrane fusion ATPase p97
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X11 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1999-09-15 |
| Detector | MARRESEARCH |
| Spacegroup name | P 6 2 2 |
| Unit cell lengths | 146.000, 146.000, 84.700 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 15.000 - 2.900 |
| R-factor | 0.224 |
| Rwork | 0.224 |
| R-free | 0.28300 |
| Structure solution method | MIRAS |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.530 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SHARP |
| Refinement software | CNS (0.5) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 3.000 |
| High resolution limit [Å] | 2.900 | 2.900 |
| Rmerge | 0.090 | 0.300 |
| Number of reflections | 12114 | |
| <I/σ(I)> | 9.7 | |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 19.3 * | 15 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 6 | 3.8-4.2 M NAFORMATE, 10% GLYCEROL, 5% PEG600, PH 5.5-6.0 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 16 (mg/ml) | |
| 2 | 1 | reservoir | sodium formate | 3.8-4.2 (M) | |
| 3 | 1 | reservoir | glycerol | 10 (%) | |
| 4 | 1 | reservoir | PEG600 | 5 (%) |
