Moradian Fatemeh, Garen Craig, Cherney Leonid, Cherney Maia, James Michael N G
Protein Structure and Function Group, Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Oct 1;62(Pt 10):986-8. doi: 10.1107/S1744309106034609. Epub 2006 Sep 30.
The gene products of two open reading frames from Mycobacterium tuberculosis (Mtb) have been crystallized using the sitting-drop vapour-diffusion method. Rv1652 encodes a putative N-acetyl-gamma-glutamyl-phosphate reductase (MtbAGPR), while the Rv1656 gene product is annotated as ornithine carbamoyltransferase (MtbOTC). Both MtbAGPR and MtbOTC were expressed in Escherichia coli, purified to homogeneity and crystallized. Native data for each crystal were collected to resolutions of 2.15 and 2.80 A, respectively. Preliminary X-ray data are presented for both enzymes.
利用坐滴气相扩散法对来自结核分枝杆菌(Mtb)的两个开放阅读框的基因产物进行了结晶。Rv1652编码一种假定的N-乙酰-γ-谷氨酰磷酸还原酶(MtbAGPR),而Rv1656基因产物被注释为鸟氨酸氨甲酰基转移酶(MtbOTC)。MtbAGPR和MtbOTC均在大肠杆菌中表达,纯化至均一性并进行结晶。分别收集了每个晶体的原生数据,分辨率分别为2.15 Å和2.80 Å。给出了这两种酶的初步X射线数据。