title: Crystallization and preliminary X-ray analysis of the yeast tRNA-thiouridine modification protein 1 (Tum1p).
abstract: Yeast tRNA-thiouridine modification protein 1 (Tum1p), a crucial component of the Urm1 system, is believed to play important roles in protein urmylation and tRNA-thiouridine modification. Previous studies have demonstrated that the conserved residue Cys259 in the C-terminal rhodanese-like domain of Tum1p is essential for these sulfur-transfer activities. Here, recombinant Tum1p protein has been cloned and overexpressed in Escherichia coli strain BL21 (DE3). After purification, crystals of Tum1p were obtained by the hanging-drop vapour-diffusion method and diffracted to 1.9 Å resolution. The preliminary X-ray data showed that the tetragonal Tum1p crystal belonged to space group I4(1), with unit-cell parameters a = b = 120.94, c = 48.35 Å. The asymmetric unit of the crystal was assumed to contain one protein molecule, giving a Matthews coefficient of 2.41 Å(3) Da(-1) and a solvent content of 49.0%.
authors.affiliation: State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University, Shanghai, People's Republic of China.
authors.forename: Rui
authors.initials: R
authors.lastname: Qiu
authors.forename: Fengbin
authors.initials: F
authors.lastname: Wang
authors.forename: Meiruo
authors.initials: M
authors.lastname: Liu
authors.forename: Zhenxing
authors.initials: Z
authors.lastname: Yang
authors.forename: Tong
authors.initials: T
authors.lastname: Wu
authors.forename: Chaoneng
authors.initials: C
authors.lastname: Ji
mesh_terms: D002352:Carrier Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D012441:Saccharomyces cerevisiae / Q000737:chemistry*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*
chemical_list: D002352:Carrier Proteins; D029701:Saccharomyces cerevisiae Proteins; C561713:Tum1 protein, S cerevisiae