1NGF
STRUCTURAL BASIS OF THE 70-KILODALTON HEAT SHOCK COGNATE PROTEIN ATP HYDROLYTIC ACTIVITY, II. STRUCTURE OF THE ACTIVE SITE WITH ADP OR ATP BOUND TO WILD TYPE AND MUTANT ATPASE FRAGMENT
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 | 6.000 - 2.170 |
| R-factor | 0.185 |
| Rwork | 0.185 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.400 |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | |
| Rmerge | 0.037 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | unknown * | 9.5 * | pH is adjusted to 9.5 with NaOH * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | PEG8000 | 20 (%) | |
| 2 | 1 | 1 | 1.0 (M) | ||
| 3 | 1 | 1 | CAPS | 50 (mM) | |
| 4 | 1 | 1 | MgATP | 1 (mM) |
