Publication Abstract from PubMed
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 P2(1), with unit-cell parameters a = 72.64, b = 61.30, c = 72.62 A, beta = 120.02 degrees at 37 K. The calculated V(M) value was acceptable when a trimer of the mutant enzyme occupied a crystallographic asymmetric unit. The resolution limit was extended to 1.45 A at BL41XU of SPring-8 at 37 K.
Crystallization of scytalone dehydratase F162A mutant in the unligated state and a preliminary X-ray diffraction study at 37 K.,Motoyama T, Nakasako M, Yamaguchi I Acta Crystallogr D Biol Crystallogr. 2002 Jan;58(Pt 1):148-50. Epub 2001, Dec 21. PMID:11752795[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
