2F9D
2.5 angstrom resolution structure of the spliceosomal protein p14 bound to region of SF3b155
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.3.1 |
| Synchrotron site | ALS |
| Beamline | 8.3.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-08-25 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.979547, 1.019859 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 101.870, 115.227, 82.536 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 76.250 - 2.500 |
| R-factor | 0.22403 |
| Rwork | 0.221 |
| R-free | 0.27562 |
| Structure solution method | MAD |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.608 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE (2.08) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 100.000 | 2.590 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.076 | 0.399 |
| Number of reflections | 17097 | |
| <I/σ(I)> | 25.5 | 2.4 |
| Completeness [%] | 99.5 | 95.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 298 | 14-18% PEG3350, MOPS buffer, 0.2M sodium formate selenomethionine derivatized SF3b155 protein, pH 6, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
