Evidence: light scattering, The protein does not elute at a position corresponding to dimer on calibrated gel filtration column. Full length protein indicated to be a dimer by SEC MALS The ...Evidence: light scattering, The protein does not elute at a position corresponding to dimer on calibrated gel filtration column. Full length protein indicated to be a dimer by SEC MALS The crystallographic dimer, when extrapolated to the full length protein using the catalytic domain crystal structure 4X47 and 2vw2 as a scaffold would introduce substantial clashes.
Mass: 18.015 Da / Num. of mol.: 488 / Source method: isolated from a natural source / Formula: H2O
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
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Sample preparation
Crystal
Density Matthews: 2.1 Å3/Da / Density % sol: 41.35 %
Crystal grow
Temperature: 293 K / Method: vapor diffusion, sitting drop Details: 0.2M ammonium chloride with 20% PEG 8000 crystal growth time was improved using micro-seeding Crystals were cryoprotected using the crystallisation condition supplemented with 25% (w/w) ...Details: 0.2M ammonium chloride with 20% PEG 8000 crystal growth time was improved using micro-seeding Crystals were cryoprotected using the crystallisation condition supplemented with 25% (w/w) glycerol crystal was co-crystallised with 10mM 2,6 sialyllactose and soaked with 100mM 2,6 sialyllactose immediately prior to freezing
Resolution: 1.3→49.91 Å / Cor.coef. Fo:Fc: 0.981 / Cor.coef. Fo:Fc free: 0.975 / SU B: 1.194 / SU ML: 0.023 / SU R Cruickshank DPI: 0.0505 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.05 / ESU R Free: 0.044 Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.1345
3481
4.9 %
RANDOM
Rwork
0.1084
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obs
0.1097
67097
83.8 %
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Solvent computation
Ion probe radii: 0.7 Å / Shrinkage radii: 0.7 Å / VDW probe radii: 1.3 Å
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