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 |