3DRY
X-ray crystal structure of human KCTD5 protein crystallized in low-salt buffer
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-D |
| Synchrotron site | APS |
| Beamline | 23-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-04-01 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97915 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 102.990, 106.791, 110.174 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 3.300 |
| R-factor | 0.26018 |
| Rwork | 0.253 |
| R-free | 0.30791 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3drx |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.276 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 3.400 |
| High resolution limit [Å] | 3.300 | 3.300 |
| Rmerge | 0.074 | 0.510 |
| Number of reflections | 20180 | |
| <I/σ(I)> | 18.14 | 1.9 |
| Completeness [%] | 99.5 | 97.6 |
| Redundancy | 5.2 | 4.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 7.5 | 0.2 M proline, 100 mM HEPES, 7% (w/v) PEG 3350, pH 7.5, VAPOR DIFFUSION |
