Abstract
Galectin-3 is an important protein in molecular signalling events involving 053
carbohydrate recognition, and an understanding of the hydrogen-bonding patterns in the
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carbohydrate binding site of its C-terminal domain (galectin-3C) is important for the
crystallography. Here we describe the production of perdeuterated human galectin-3C and
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reduced data collection times. Furthermore, we describe protocols for complete removal of the lactose that is necessary for production of large crystals of apo-galectin-3C suitable for neutron diffraction. We have collected five datasets at three different neutron sources from galectin-3C crystals of similar volume. We have been able to merge two of these to generate
successive improvement in crystal size by development of a crystal growth protocol involving
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010 insights into the crystal volumes and data collection times necessary for the same system at 011
an almost complete neutron data set for the galectin-3C:lactose complex. These datasets give
sources with different technologies and data collection strategies, and these insights are applicable to other systems.
