{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["61(Pt 12)"],"submitter":["Miura-Ohnuma J"],"pubmed_abstract":["N-Acetyl-gamma-glutamyl-phosphate reductase (AGPR) catalyzes the third step in an eight-step arginine-biosynthetic pathway that starts with glutamate. This enzyme converts N-acetyl-gamma-glutamyl phosphate to N-acetylglutamate-gamma-semialdehyde by an NADPH-dependent reductive dephosphorylation. AGPR from Oryza sativa (OsAGPR) was expressed in Escherichia coli at 291 K as a soluble fusion protein with an upstream thioredoxin-hexahistidine [Trx-(His)6] extension. OsAGPR(Ala50-Pro366) was purified and crystals were obtained using the sitting-drop vapour-diffusion method at 293 K and diffract X-rays to at least 1.8 A resolution. They belong to the hexagonal space group P6(1), with unit-cell parameters a = 86.11, c = 316.3 A."],"journal":["Acta crystallographica. Section F, Structural biology and crystallization communications"],"pagination":["1058-61"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC1978146"],"repository":["biostudies-literature"],"pubmed_title":["Improved expression, purification and crystallization of a putative N-acetyl-gamma-glutamyl-phosphate reductase from rice (Oryza sativa)."],"pmcid":["PMC1978146"],"pubmed_authors":["Nonaka T","Kita A","Murata K","Miura-Ohnuma J","Katoh S","Miki K","Katoh E"],"additional_accession":[]},"is_claimable":false,"name":"Improved expression, purification and crystallization of a putative N-acetyl-gamma-glutamyl-phosphate reductase from rice (Oryza sativa).","description":"N-Acetyl-gamma-glutamyl-phosphate reductase (AGPR) catalyzes the third step in an eight-step arginine-biosynthetic pathway that starts with glutamate. This enzyme converts N-acetyl-gamma-glutamyl phosphate to N-acetylglutamate-gamma-semialdehyde by an NADPH-dependent reductive dephosphorylation. AGPR from Oryza sativa (OsAGPR) was expressed in Escherichia coli at 291 K as a soluble fusion protein with an upstream thioredoxin-hexahistidine [Trx-(His)6] extension. OsAGPR(Ala50-Pro366) was purified and crystals were obtained using the sitting-drop vapour-diffusion method at 293 K and diffract X-rays to at least 1.8 A resolution. They belong to the hexagonal space group P6(1), with unit-cell parameters a = 86.11, c = 316.3 A.","dates":{"release":"2005-01-01T00:00:00Z","publication":"2005 Dec","modification":"2021-02-20T09:48:40Z","creation":"2019-03-27T00:13:44Z"},"accession":"S-EPMC1978146","cross_references":{"pubmed":["16511234"],"doi":["10.1107/S1744309105035384","10.1107/s1744309105035384"]}}