Open AccessCrystallization and preliminary X‐ray analysis of L‐serine 3‐dehydrogenase complexed with NADP + from the hyperthermophilic archaeon Pyrobaculum calidifontis
Author(s) -
Yoneda Kazunari,
Sakuraba Haruhiko,
Araki Tomohiro,
Shibata Takeshi,
Nikki Takahiro,
Ohshima Toshihisa
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112051391
Subject(s) - ammonium sulfate , monoclinic crystal system , dehydrogenase , crystallography , nad+ kinase , chemistry , materials science , nuclear chemistry , biochemistry , crystal structure , enzyme , chromatography
An NAD(P) + ‐dependent L‐serine 3‐dehydrogenase from the hyperthermophilic archaeon Pyrobaculum calidifontis was crystallized using the sitting‐drop vapour‐diffusion method with ammonium sulfate as the precipitant. The crystals belonged to the monoclinic space group C 2, with unit‐cell parameters a = 120.81, b = 57.40, c = 56.37 Å, β = 106.88°. Diffraction data were collected to 1.57 Å resolution on beamline NE3A at the Photon Factory. The overall R merge was 4.2% and the data completeness was 90.1%.