Crystallization and preliminary crystallographic studies of five crystal forms of Escherichia coli L-­asparaginase II (Asp90Glu mutant)

E. coli L-asparaginase II with a Asp90Glu mutation in the active site has been crystallized in five polymorphic forms.

Crystallization and preliminary crystallographic studies of Streptococcus pyogenes cysteine protease precursor

Wild-type cysteine protease precursor from the human pathogen S. pyogenes was obtained in the form of crystalline flakes from which X-ray diffraction data were collected to 3.15 Å resolution at 100 K using synchrotron radiation. The crystals are monoclinic, space group P2₁, with unit-cell parameters a = 41.6, b = 136.0, c = 156.7 Å, β = 95.7°, and contain four copies of the protein in the asymmetric unit.