2WBD
FRUCTOSE-1,6-BISPHOSPHATASE(D-FRUCTOSE-1,6-BISPHOSPHATE-1- PHOSPHOHYDROLASE) (E.C.3.1.3.11) COMPLEXED WITH AN AMP SITE INHIBITOR
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 120 |
| Detector technology | CCD |
| Collection date | 2005-11-13 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 66.842, 285.402, 83.552 |
| Unit cell angles | 90.00, 97.57, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.400 |
| R-factor | 0.22276 |
| Rwork | 0.220 |
| R-free | 0.27684 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2wbb |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.348 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Refinement software | REFMAC (5.5.0070) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.500 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.100 | 0.490 |
| Number of reflections | 237087 | |
| <I/σ(I)> | 8.28 | 2.4 |
| Completeness [%] | 99.1 | 98.6 |
| Redundancy | 1.95 | 1.95 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 0.1M AMMONIUM ACETATE, 0.1M HEPES PH 7.0, 15% PEG 3350 |
