1IDP

Crystallization of scytalone dehydratase F162A mutant in the unligated state and a preliminary X-ray diffraction study at 37 K

(2002) Acta Crystallogr D Biol Crystallogr 58: 148-150

• PubMed: 11752795 Search on PubMed
• DOI: https://doi.org/10.1107/s0907444901017371
• Primary Citation of Related Structures:  
  1IDP


• PubMed Abstract: 
  

  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.

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Organizational Affiliation: 

RIKEN (The Institute of Physical and Chemical Research), 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.