3ESK
Structure of HOP TPR2A domain in complex with the non-cognate Hsc70 peptide ligand
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2005-10-28 |
Detector | MAR scanner 345 mm plate |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 73.459, 48.023, 37.896 |
Unit cell angles | 90.00, 91.56, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.050 |
R-factor | 0.183 |
Rwork | 0.177 |
R-free | 0.24400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1elr |
RMSD bond length | 0.023 |
RMSD bond angle | 1.685 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | AMoRE |
Refinement software | REFMAC (5.5.0036) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.100 |
High resolution limit [Å] | 2.050 | 2.050 |
Number of reflections | 8178 | |
<I/σ(I)> | 13.8 | 3.9 |
Completeness [%] | 94.7 | 81.2 |
Redundancy | 2.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8.5 | 298 | TRIS pH 8.5, PEG MME 2000, NiCl2, Xylitol, VAPOR DIFFUSION, temperature 298K |