2FUS
MUTATIONS OF FUMARASE THAT DISTINGUISH BETWEEN THE ACTIVE SITE AND A NEARBY DICARBOXYLIC ACID BINDING SITE
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH2R |
| Temperature [K] | 298 |
| Detector technology | AREA DETECTOR |
| Collection date | 1996-02 |
| Detector | SIEMENS |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 104.160, 220.050, 86.650 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 2.200 |
| R-factor | 0.178 |
| Rwork | 0.178 |
| R-free | 0.22900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1fuo |
| RMSD bond length | 0.007 |
| RMSD bond angle | 21.250 * |
| Data reduction software | XENGEN |
| Data scaling software | XENGEN |
| Phasing software | X-PLOR (3.1) |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 8.000 | 2.060 |
| High resolution limit [Å] | 1.980 | 1.980 |
| Rmerge | 0.070 | 0.610 |
| Number of reflections | 60762 | |
| <I/σ(I)> | 7.4 | 0.435 |
| Completeness [%] | 88.0 | 46 |
| Redundancy | 4.3 | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | unknown * | 6 * | PROTEIN WAS CRYSTALLIZED FROM 150MM CITRATE PH 5.0 AND 14% PEG 4000 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | citrate | 300 (mM) | |
| 2 | 1 | 1 | PEG3350 | 12-14 (%(w/v)) |
