Scytalone dehydratase variant F162A, in which Phe162 in the C-terminal region was replaced with alanine, was crystallized with polyethylene glycol 4000. Because the crystal was radiation-sensitive, the diffraction data were collected at cryogenic temperatures. The crystal belonged to monoclinic space group P21, with unit-cell parameters a = 72.64, b = 61.30, c = 72.62 Å, β = 120.02° at 37 K. The calculated VM value was acceptable when a trimer of the mutant enzyme occupied a crystallographic asymmetric unit. The resolution limit was extended to 1.45 Å at BL41XU of SPring-8 at 37 K.
|Number of pages||3|
|Journal||Acta Crystallographica Section D: Biological Crystallography|
|Publication status||Published - 2002 Feb 6|
ASJC Scopus subject areas
- Structural Biology