title: Crystallization and diffraction analysis of Sm23: an SGNH-family arylesterase from Sinorhizobium meliloti 1021.
abstract: Industrial demand for active biocatalysts with desirable biochemical properties is constantly increasing and the discovery and characterization of novel esterases is potentially useful for industrial processes. Here, X-ray crystallographic studies of an (R)-specific SGNH arylesterase (Sm23) from Sinorhizobium meliloti 1021 are reported. The recombinant protein was expressed in Escherichia coli with a His tag and purified to homogeneity. Sm23 was crystallized using 0.2 M magnesium formate as a precipitant and X-ray diffraction data were collected to a resolution of 2.2 Å with an R(merge) of 6.9%. The crystals of SM23 belonged to the I-centred tetragonal space group I4(1)22, with unit-cell parameters a = b = 126.6, c = 190.9 Å. A molecular-replacement solution was obtained using the crystal structure of arylesterase from Mycobacterium smegmatis as a template.
authors.affiliation: Department of Molecular Science and Technology, Graduate School of Interdisciplinary Programs, Ajou University, Suwon 443-749, Republic of Korea.
authors.forename: Heejin
authors.initials: H
authors.lastname: Hwang
authors.forename: Sungsoo
authors.initials: S
authors.lastname: Kim
authors.forename: Sohyun
authors.initials: S
authors.lastname: Park
authors.forename: Tri Duc
authors.initials: TD
authors.lastname: Ngo
authors.forename: Kyeong Kyu
authors.initials: KK
authors.lastname: Kim
authors.forename: T Doohun
authors.initials: TD
authors.lastname: Kim
mesh_terms: D000947:Antigens, Helminth / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D016962:Sinorhizobium meliloti / Q000201:enzymology*
chemical_list: D000947:Antigens, Helminth; C067614:antigen Sm23, Schistosoma