1G99
AN ANCIENT ENZYME: ACETATE KINASE FROM METHANOSARCINA THERMOPHILA
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 297 |
| Detector technology | IMAGE PLATE |
| Collection date | 1996-09-09 |
| Detector | RIGAKU RAXIS IIC |
| Wavelength(s) | 1.5418 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 181.300, 67.400, 82.600 |
| Unit cell angles | 90.00, 102.90, 90.00 |
Refinement procedure
| Resolution | 36.000 - 2.500 |
| Rwork | 0.147 |
| R-free | 0.18770 |
| Structure solution method | MIR |
| RMSD bond length | 0.012 |
| RMSD bond angle | 23.172 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MLPHARE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.700 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Number of reflections | 32857 | |
| Completeness [%] | 97.0 | 95 |
| Redundancy | 5.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | Buss, K.A., (1997) Protein Sci., 6, 2659. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | acetate | 0.0049mg | |
| 2 | 1 | drop | ATP | 0.75 (mM) | |
| 3 | 1 | drop | 0.75 (mM) | ||
| 4 | 1 | drop | ammonium sulfate | 315 (mM) | |
| 5 | 1 | drop | dithiothreitol | 0.8 (mM) | |
| 6 | 1 | drop | sodium HEPES | 25 (mM) | |
| 7 | 1 | reservoir | ammonium sulfate | 1.7 (M) |
