4CGU
Full length Tah1 bound to yeast PIH1 and HSP90 peptide SRMEEVD
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 HF |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-03-15 |
| Detector | RIGAKU CCD |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 56.010, 78.380, 98.790 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.190 - 2.110 |
| R-factor | 0.1708 |
| Rwork | 0.169 |
| R-free | 0.21010 |
| Structure solution method | SAD |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.913 |
| Data reduction software | xia2 |
| Data scaling software | xia2 |
| Phasing software | SHELX |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 39.190 | 2.160 |
| High resolution limit [Å] | 2.110 | 2.110 |
| Rmerge | 0.050 | 0.210 |
| Number of reflections | 12533 | |
| <I/σ(I)> | 83.7 | 5.7 |
| Completeness [%] | 97.4 | 67.3 |
| Redundancy | 56.6 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7 | pH 7 |






