嗜热栖热菌II类果糖-1,6-二磷酸醛缩酶的结晶及初步X射线分析

Crystallization and preliminary X-ray analysis of class II fructose-1,6-bisphosphate aldolase from Thermus caldophilus.

作者信息

Lee Jun Hyuck, Im Young Jun, Rho Seong-Hwan, Park Seong Ho, Kim Mun-Kyoung, Cho Su Jin, Kim Tae-Yeon, Oh Jin Hwan, Shin Hyun-Jae, Lee Dae-Sil, Eom Soo Hyun

机构信息

Department of Life Science, Kwangju Institute of Science & Technology, Gwangju 500-712, Korea.

出版信息

Protein Pept Lett. 2003 Oct;10(5):511-5. doi: 10.2174/0929866033478735.

DOI:10.2174/0929866033478735

PMID:14561141

Abstract

In this study, we have crystallized class II fructose-1,6-bisphosphate aldolase (FBA) from Thermus caldophilus (Tca). Purified Tca FBA is a tetrameric enzyme of 305 residues, which crystallizes in the space group P2(1)2(1)2(1) (cell dimensions a = 98.9, b = 113.1, c = 115.7 A), with four molecules in the asymmetric unit. A complete diffraction data set was obtained from orthorhombic crystals at resolution of 2.2 A.

摘要

在本研究中，我们已成功结晶了嗜热栖热菌（Tca）的II类果糖-1,6-二磷酸醛缩酶（FBA）。纯化后的Tca FBA是一种由305个残基组成的四聚体酶，它在空间群P2(1)2(1)2(1)（晶胞参数a = 98.9，b = 113.1，c = 115.7 Å）中结晶，不对称单元中有四个分子。从正交晶体获得了分辨率为2.2 Å的完整衍射数据集。