Crystallization and preliminary X-ray diffraction analysis of a flavoenzyme amine dehydrogenase/oxidase from Pyrococcus furiosus DSM 3638.
A flavoprotein amine dehydrogenase/oxidase with subunit molecular weights of 54.8 kDa (alpha-subunit) and 42.4 kDa (beta-subunit) and specificity for L-proline was cloned from the genomic DNA of the hyperthermophilic marine archaeon Pyrococcus furiosus DSM 3638. The enzyme was overexpressed in Escherichia coli and purified to homogeneity. The enzyme was crystallized using the sitting-drop vapour-diffusion technique. Diffraction data from two different crystal forms were collected to 3.3 and 3.6 A, respectively, using synchrotron radiation. Both crystals belonged to space group P1, with unit-cell parameters a = 91.3, b = 136.3, c = 203.8 A, alpha = 94.5, beta = 99.4, gamma = 102.7 degrees and a = 93.7, b = 116.3, c = 126.9 A, alpha = 97.3, beta = 99.9, gamma = 104.6 degrees.
Monaghan
Phillip J
PJ
Department of Biochemistry, University of Leicester, Leicester LE1 7RH, England.
Leys
David
D
Scrutton
Nigel S
NS
D003460:Crystallization; D008995:Monoamine Oxidase / Q000737:chemistry*; D020027:Pyrococcus furiosus / Q000145:classification* / Q000201:enzymology*; D011994:Recombinant Proteins / Q000737:chemistry; D014961:X-Ray Diffraction
D011994:Recombinant Proteins; D008995:Monoamine Oxidase