Crystallization and preliminary X-ray crystallographic studies of succinic semialdehyde dehydrogenase from Streptococcus pyogenes

Eun Hyuk Jang, Jong Eun Lim, Young Min Chi, Ki Seog Lee

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2 Citations (Scopus)


Succinic semialdehyde dehydrogenase (SSADH) plays a critical role in the metabolism of the inhibitory neurotransmitter γ-aminobutyric acid (GABA) and catalyzes the NAD(P) +-coupled oxidation of succinic semialdehyde (SSA) to succinic acid (SA). SSADH from Streptococcus pyogenes has been purified and crystallized as the apoenzyme and in a complex with NAD +. The crystals of native and NAD +-complexed SSADH diffracted to resolutions of 1.6 and 1.7 Å, respectively, using a synchrotron-radiation source. Both crystals belonged to the orthorhombic space group P2 12 12 1, with unit-cell parameters a = 93.3, b = 100.3, c = 105.1 Å for the native crystal and a = 93.3, b = 100.3, c = 105.0 Å for the complex crystal. Preliminary molecular replacement confirmed the presence of one dimer in both crystals, corresponding to a Matthews coefficient (V M) of 2.37 Å 3 Da -1 and a solvent content of 48.0%.

Original languageEnglish
Pages (from-to)288-291
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number3
Publication statusPublished - 2012 Mar 1



  • GabD
  • NAD
  • Streptococcus pyogenes
  • succinic semialdehyde dehydrogenase

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Structural Biology
  • Genetics
  • Condensed Matter Physics

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