4CGQ
Full length Tah1 bound to 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 | 2013-04-10 |
| Detector | RIGAKU CCD |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 62.790, 62.790, 57.900 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 13.840 - 2.000 |
| R-factor | 0.165 |
| Rwork | 0.163 |
| R-free | 0.21020 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | IN-HOUSE STRUCTURE |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.791 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 13.840 | 2.050 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.180 | 0.670 |
| Number of reflections | 8230 | |
| <I/σ(I)> | 7.9 | 3 |
| Completeness [%] | 99.7 | 100 |
| Redundancy | 10.3 | 10 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7 | pH 7 |
