3PRA
Structural analysis of protein folding by the Methanococcus jannaschii chaperone FKBP26
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X4A |
| Synchrotron site | NSLS |
| Beamline | X4A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2000-10-01 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 45.984, 67.886, 54.466 |
| Unit cell angles | 90.00, 95.29, 90.00 |
Refinement procedure
| Resolution | 19.760 - 2.400 |
| R-factor | 0.2371 |
| Rwork | 0.234 |
| R-free | 0.29110 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.227 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 30.000 | 30.000 | 2.440 |
| High resolution limit [Å] | 2.400 | 6.490 | 2.400 |
| Rmerge | 0.054 | 0.044 | 0.239 |
| Number of reflections | 13060 | ||
| <I/σ(I)> | 25.4 | ||
| Completeness [%] | 99.4 | 92.1 | 100 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | hanging drop | 298 | 6% PMME2K, 0.2 M (NH4)2SO4, pH 100 mM HEPES, pH 7.25, hanging drop, temperature 298K |
