A set of 60 proteins from Streptococcus pneumonia were selected and produced as SeMet labelled protein.  These proteins were put though very limited crystallisation screening and simultaneously analysed for thermal stability using differential scanning fluorimetry.  From an initial pass of 96 conditions, surprisingly few of the proteins yielded crystals, and of those that showed some sign of crystallisability in the initial screen less than half produced harvestable crystals.  There is a wide variation in the thermal stability of the proteins, those that produced crystals also behaved well in the thermal melts.