1ELR
Crystal structure of the TPR2A domain of HOP in complex with the HSP90 peptide MEEVD
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-3 |
Synchrotron site | ESRF |
Beamline | ID14-3 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1999-10-05 |
Detector | MARRESEARCH |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 73.280, 48.270, 38.060 |
Unit cell angles | 90.00, 91.30, 90.00 |
Refinement procedure
Resolution | 9.930 - 1.900 |
R-factor | 0.181 |
Rwork | 0.181 |
R-free | 0.21900 |
RMSD bond length | 0.008 |
RMSD bond angle | 1.200 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | MLPHARE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 1.950 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.038 | 0.068 |
<I/σ(I)> | 22.8 | |
Completeness [%] | 97.1 | 91.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 * | 20 * | PEG MME 2000, TRIS, Nickel chloride, Xylitol, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein-peptide complex | 15 (mg/ml) | |
2 | 1 | drop | Tris | 50 (mM) | |
3 | 1 | drop | DDT | 2 (mM) | |
4 | 1 | reservoir | Tris | 100 (mM) | |
5 | 1 | reservoir | PEG2000MME | 20 (%(w/v)) | |
6 | 1 | reservoir | 5 (mM) | ||
7 | 1 | reservoir | xylitol | 10 (%(w/v)) |