title: Crystallization and preliminary X-ray diffraction analysis of MJ0458, an adenylate kinase from Methanocaldococcus jannaschii.
abstract: Adenylate kinase plays a very important role in regulating adenylate species in the cell. Methanocaldococcus jannaschii is a rich resource of unique enzymes. Here, MJ0458, an adenylate kinase from M. jannaschii, was crystallized. A set of X-ray diffraction data to 2.70 Å resolution was collected on beamline BL-17U of the Shanghai Synchrotron Radiation Facility (SSRF). The crystal belonged to space group P4(1)2(1)2 or P4(3)2(1)2. The unit-cell parameters were a = b = 76.18, c = 238.70 Å, α = β = γ = 90°.
authors.affiliation: School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230026, People's Republic of China.
authors.forename: Xiao
authors.initials: X
authors.lastname: Wang
authors.forename: Ye
authors.initials: Y
authors.lastname: Yuan
authors.forename: Maikun
authors.initials: M
authors.lastname: Teng
authors.forename: Liwen
authors.initials: L
authors.lastname: Niu
authors.forename: Yongxiang
authors.initials: Y
authors.lastname: Gao
mesh_terms: D000263:Adenylate Kinase / Q000737:chemistry*; D003460:Crystallization; D004591:Electrophoresis, Polyacrylamide Gel; D063747:Methanocaldococcus / Q000201:enzymology*; D011994:Recombinant Proteins / Q000737:chemistry; D014961:X-Ray Diffraction
chemical_list: D011994:Recombinant Proteins; D000263:Adenylate Kinase
keywords: MJ0458; Methanocaldococcus jannaschii; adenylate kinase