Open AccessCrystallization and preliminary X‐ray diffraction analysis of MJ0458, an adenylate kinase from Methanocaldococcus jannaschii
Author(s) -
Wang Xiao,
Yuan Ye,
Teng Maikun,
Niu Liwen,
Gao Yongxiang
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113026638
Subject(s) - adenylate kinase , crystallography , x ray , crystallization , resolution (logic) , crystal (programming language) , diffraction , x ray crystallography , materials science , chemistry , biology , enzyme , physics , biochemistry , optics , organic chemistry , computer science , programming language , artificial intelligence
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 P 4 1 2 1 2 or P 4 3 2 1 2. The unit‐cell parameters were a = b = 76.18, c = 238.70 Å, α = β = γ = 90°.