Publication: Crystallization and preliminary X-ray crystallographic analysis of D-phenylglycine aminotransferase from Pseudornonas stutzeri ST201
Issued Date
2003-05-01
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ISSN
09074449
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2-s2.0-0038181383
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Mahidol University
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SCOPUS
Bibliographic Citation
Acta Crystallographica - Section D Biological Crystallography. Vol.59, No.5 (2003), 953-954
Suggested Citation
Palangpon Kongsaeree, Chariwat Samanchart, Poramaet Laowanapiban, Suthep Wiyakrutta, Vithaya Meevootisom Crystallization and preliminary X-ray crystallographic analysis of D-phenylglycine aminotransferase from Pseudornonas stutzeri ST201. Acta Crystallographica - Section D Biological Crystallography. Vol.59, No.5 (2003), 953-954. doi:10.1107/S0907444903006498 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/20729
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Title
Crystallization and preliminary X-ray crystallographic analysis of D-phenylglycine aminotransferase from Pseudornonas stutzeri ST201
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Abstract
D-Phenylglycine aminotransferase (D-PhgAT) catalyzes the reversible transamination of D-phenylglycine to L-glutamate with 2-oxoglutarate as the amino-group acceptor. Crystals of substrate-free Pseudomonas stutzeri D-PhgAT bound to the cofactor pyridoxal-5′-phosphate (PLP) were obtained by the hanging-drop vapour-diffusion method using ammonium sulfate as a precipitant. The crystals belong to space group P3121 or P3221, with unit-cell parameters a = b = 75.155, c = 147.554 Å. The asymmetric unit contains one molecule of D-PhgAT and has a solvent content of 50.0%. A complete native X-ray diffraction data set was collected from a single crystal at 100 K to a resolution of 2.3 Å.