3PIG
beta-fructofuranosidase from Bifidobacterium longum
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.2 |
| Synchrotron site | BESSY |
| Beamline | 14.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-05-21 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.9184 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 87.117, 87.117, 223.942 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 75.450 - 1.870 |
| R-factor | 0.14989 |
| Rwork | 0.149 |
| R-free | 0.19866 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1W2T and 1Y4W |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.687 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0091) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 1.940 |
| High resolution limit [Å] | 1.870 | 1.870 |
| Rmerge | 0.090 | 0.445 |
| Number of reflections | 81348 | |
| <I/σ(I)> | 19.19 | 2 |
| Completeness [%] | 98.6 | 87.3 |
| Redundancy | 6.1 | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 0.4M ammonium chloride, 18% PEG 3350, 0.1M MES pH 7.0, protein concentration 11 mg/ml, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
