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 |