{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["68(Pt 3)"],"submitter":["Jang EH"],"pubmed_abstract":["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(1)2(1)2(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%."],"journal":["Acta crystallographica. Section F, Structural biology and crystallization communications"],"pagination":["288-91"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3310532"],"repository":["biostudies-literature"],"pubmed_title":["Crystallization and preliminary X-ray crystallographic studies of succinic semialdehyde dehydrogenase from Streptococcus pyogenes."],"pmcid":["PMC3310532"],"pubmed_authors":["Lim JE","Lee KS","Jang EH","Chi YM"],"additional_accession":[]},"is_claimable":false,"name":"Crystallization and preliminary X-ray crystallographic studies of succinic semialdehyde dehydrogenase from Streptococcus pyogenes.","description":"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(1)2(1)2(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%.","dates":{"release":"2012-01-01T00:00:00Z","publication":"2012 Mar","modification":"2025-04-21T14:20:37.363Z","creation":"2019-03-27T00:01:32Z"},"accession":"S-EPMC3310532","cross_references":{"pubmed":["22442224"],"doi":["10.1107/S1744309111052055","10.1107/s1744309111052055"]}}