3RKV
C-terminal domain of protein C56C10.10, a putative peptidylprolyl isomerase, from Caenorhabditis elegans
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-06-19 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9792 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 42.025, 84.674, 110.731 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 42.300 - 2.410 |
| R-factor | 0.2401 |
| Rwork | 0.237 |
| R-free | 0.30050 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2fbn |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.646 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 42.400 | 50.000 | 2.460 |
| High resolution limit [Å] | 2.410 | 6.560 | 2.420 |
| Rmerge | 0.087 | 0.050 | 0.815 |
| Number of reflections | 7946 | ||
| <I/σ(I)> | 9.2 | 1.98 | |
| Completeness [%] | 100.0 | 100 | 100 |
| Redundancy | 9.3 | 8.4 | 7.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 9.5 | 297 | 40% MPD, 0.1 M CHES , pH 9.5, VAPOR DIFFUSION, SITTING DROP, temperature 297K |
