1FIY
THREE-DIMENSIONAL STRUCTURE OF PHOSPHOENOLPYRUVATE CARBOXYLASE FROM ESCHERICHIA COLI AT 2.8 A RESOLUTION
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-18B |
| Synchrotron site | Photon Factory |
| Beamline | BL-18B |
| Temperature [K] | 298 |
| Detector technology | DIFFRACTOMETER |
| Collection date | 1996-12-15 |
| Detector | WEISSENBERG |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 117.600, 248.400, 82.700 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 2.800 |
| R-factor | 0.219 |
| R-free | 0.25900 |
| Structure solution method | MULTIPLE ISOMORPHOUS REPLACEMENT |
| RMSD bond length | 0.011 |
| RMSD bond angle | 0.026 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MLPHARE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 100.000 | 2.900 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.069 | 0.251 |
| Number of reflections | 28509 | |
| Completeness [%] | 93.3 | 87.5 |
| Redundancy | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 7.4 * | pH 8.0 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 10 | 1 | reservoir | PEG300 | 15 (%(w/v)) | |
| 11 | 1 | reservoir | Tris-HCl | 50 (mM) | |
| 2 | 1 | drop | Tris-HCl | 50 (mM) | |
| 3 | 1 | drop | sodium-L-aspartate | 6 (mM) | |
| 4 | 1 | drop | 45 (mM) | ||
| 5 | 1 | drop | dithiothreitol | 0.6 (mM) | |
| 6 | 1 | drop | PEG300 | 10 (%(w/v)) | |
| 7 | 1 | reservoir | L-aspartate | 2.5 (mM) | |
| 8 | 1 | reservoir | 90 (mM) | ||
| 9 | 1 | reservoir | dithiothreitol | 0.25 (mM) |
