2WBB
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 | 2005-04-10 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 64.730, 278.563, 82.702 |
| Unit cell angles | 90.00, 97.87, 90.00 |
Refinement procedure
| Resolution | 29.700 - 2.220 |
| R-factor | 0.202 |
| Rwork | 0.199 |
| R-free | 0.24800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1fta |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.316 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.340 |
| High resolution limit [Å] | 2.200 | 2.210 |
| Rmerge | 0.070 | 0.320 |
| Number of reflections | 137428 | |
| <I/σ(I)> | 13.15 | 2.2 |
| Completeness [%] | 95.3 | 71.8 |
| Redundancy | 3.4 | 1.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 0.1M AMMONIUM ACETATE 0.1M HEPES PH7 25% PEG 3350 |
