产氨棒杆菌FAD合成酶的结晶及初步X射线衍射研究。
Crystallization and preliminary X-ray diffraction studies of FAD synthetase from Corynebacterium ammoniagenes.
作者信息
Herguedas Beatriz, Martínez-Júlvez Marta, Frago Susana, Medina Milagros, Hermoso Juan A
机构信息
Departamento de Bioquímica y Biología Molecular y Celular, Facultad de Ciencias, and Institute of Biocomputation and Physics of Complex Systems, Universidad de Zaragoza, 50009 Zaragoza, Spain.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Dec 1;65(Pt 12):1285-8. doi: 10.1107/S1744309109044789. Epub 2009 Nov 27.
Abstract
FAD synthetase from Corynebacterium ammoniagenes (CaFADS), a prokaryotic bifunctional enzyme that catalyses the phosphorylation of riboflavin as well as the adenylylation of FMN, has been crystallized using the hanging-drop vapour-diffusion method at 277 K. Diffraction-quality cubic crystals of native and selenomethionine-labelled (SeMet-CaFADS) protein belonged to the cubic space group P2(1)3, with unit-cell parameters a = b = c = 133.47 A and a = b = c = 133.40 A, respectively. Data sets for native and SeMet-containing crystals were collected to 1.95 and 2.42 A resolution, respectively.
摘要
产氨棒杆菌（CaFADS）的黄素腺嘌呤二核苷酸（FAD）合成酶是一种原核双功能酶，可催化核黄素的磷酸化以及黄素单核苷酸（FMN）的腺苷酸化。该酶已采用悬滴气相扩散法在277 K下结晶。天然蛋白和硒代蛋氨酸标记（SeMet-CaFADS）蛋白的衍射质量立方晶体分别属于立方空间群P2(1)3，晶胞参数a = b = c = 133.47 Å和a = b = c = 133.40 Å。天然晶体和含SeMet晶体的数据集分别收集到1.95 Å和2.42 Å分辨率。
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