3MBF
Crystal structure of fructose bisphosphate aldolase from Encephalitozoon cuniculi, bound to fructose 1,6-bisphosphate
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL7-1 |
Synchrotron site | SSRL |
Beamline | BL7-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-03-19 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.977400 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 121.460, 135.820, 61.540 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 28.030 - 2.370 |
R-factor | 0.167 |
Rwork | 0.165 |
R-free | 0.20800 |
Structure solution method | FOURIER SYNTHESIS |
Starting model (for MR) | 3mdb |
RMSD bond length | 0.016 |
RMSD bond angle | 1.499 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | REFMAC |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 28.030 | 2.430 |
High resolution limit [Å] | 2.370 | 2.370 |
Rmerge | 0.081 | 0.479 |
Number of reflections | 21046 | |
<I/σ(I)> | 15.35 | 3.2 |
Completeness [%] | 99.7 | 99.6 |
Redundancy | 4.4 | 4.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 290 | BASED ON PACT SCREEN CONDITION F10 WITHOUT NAKHPO4: 100MM BIS-TRIS PROPANE PH 6.5, 20% PEG 3350, 20 MM FRUCTOSE 1,6-BISPHOSPHATE, PROTEIN AT 24.7 MG/ML, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K |