1ATS
THREONINE 204 OF THE CHAPERONE PROTEIN HSC70 INFLUENCES THE STRUCTURE OF THE ACTIVE SITE BUT IS NOT ESSENTIAL FOR ATP HYDROLYSIS
Experimental procedure
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 145.300, 65.000, 46.900 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | ? - 2.120 * |
| R-factor | 0.209 |
| Rwork | 0.209 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.420 |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 2.120 * |
| Rmerge | 0.043 * |
| Number of reflections | 12889 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | other * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | PEG8000 | 20 (%) | |
| 2 | 1 | reservoir | 1 (M) |
