1KP8
Structural Basis for GroEL-assisted Protein Folding from the Crystal Structure of (GroEL-KMgATP)14 at 2.0 A Resolution
Replaces: 1DERExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X25 |
| Synchrotron site | NSLS |
| Beamline | X25 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1994-09-01 |
| Detector | FUJI |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 135.571, 260.112, 150.200 |
| Unit cell angles | 90.00, 101.14, 90.00 |
Refinement procedure
| Resolution | 39.890 - 2.000 |
| Rwork | 0.243 |
| R-free | 0.25790 * |
| RMSD bond length | 0.006 |
| RMSD bond angle | 20.000 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 40.000 |
| High resolution limit [Å] | 2.000 |
| Rmerge | 0.096 |
| Total number of observations | 645898 * |
| Number of reflections | 540791 * |
| Completeness [%] | 99.1 * |
| Redundancy | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | other * | Ranson, N.A., (1998) Biochem. J., 333, 233. * |
