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A methodology and an instrument for the temperature-controlled optimization of crystal growth are described. The technique finds application in the growth of large high-quality crystals for neutron crystallography.

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Slit2 is a large multidomain protein containing an unusual domain organization of four tandem leucine-rich repeat (LRR) domains at its N-terminus. Here, the crystallization of the second and third LRR domains from human Slit2 and the structure of the third LRR domain are presented.
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