Kudo N, Allen M D, Koike H, Katsuya Y, Suzuki M
AIST-NIBHT CREST Centre of Structural Biology, 1-1 Higashi, Tsukuba 305-0046, Japan.
Acta Crystallogr D Biol Crystallogr. 2001 Mar;57(Pt 3):469-71. doi: 10.1107/s0907444900020369.
A protein belonging to the Lrp/AsnC transcription-factor family, pot1216151, from the hyperthermophilic archaeon Pyrococcus sp. OT3 was crystallized. In Escherichia coli, leucine-responsive protein (Lrp) and AsnC regulate a number of metabolic genes. The crystals of pot1216151 diffracted to 2.3 A using a conventional X-ray source and to 1.8 A using a synchrotron-radiation source. The space group was identified to be P3(1)21 or P3(2)21, with unit-cell parameters a = b = 96.9, c = 98.5 A. In combination with diffraction data obtained from K(2)[Pt(CN)(6)] and K(AuCl(4)) derivatives, an electron-density map was calculated at a resolution of 3.0 A. Four monomers were identified in the asymmetric unit, with four beta-strands and two alpha-helices in each monomer.
对来自嗜热古菌嗜热栖热菌OT3的一种属于Lrp/AsnC转录因子家族的蛋白质pot1216151进行了结晶。在大肠杆菌中，亮氨酸应答蛋白（Lrp）和AsnC调控许多代谢基因。使用常规X射线源时，pot1216151的晶体衍射分辨率为2.3 Å，使用同步辐射源时衍射分辨率为1.8 Å。确定空间群为P3(1)21或P3(2)21，晶胞参数a = b = 96.9，c = 98.5 Å。结合从K(2)[Pt(CN)(6)]和K(AuCl(4))衍生物获得的衍射数据，计算出分辨率为3.0 Å的电子密度图。在不对称单元中鉴定出四个单体，每个单体中有四条β链和两条α螺旋。
