%0 Journal Article
%A Li, Long
%A Adachi, Motoyasu
%A Yu, Jian
%A Kato, Koji
%A Shinoda, Akira
%A Ostermann, Andreas
%A Schrader, Tobias E.
%A Ose, Toyoyuki
%A Yao, Min
%T Neutron crystallographic study of heterotrimeric glutamine amidotransferase CAB
%J Acta crystallographica / F Structural biology communications Section F
%V 75
%N 3
%@ 2053-230X
%C Oxford [u.a.]
%I Blackwell
%M FZJ-2020-00321
%P 193 - 196
%D 2019
%X Heterotrimeric glutamine amidotransferase CAB (GatCAB) possesses anammonia-self-sufficient mechanism in which ammonia is produced and usedin the inner complex by GatA and GatB, respectively. The X-ray structure ofGatCAB revealed that the two identified active sites of GatA and GatB aremarkedly distant, but are connected in the complex by a channel of 30 A ˚ inlength. In order to clarify whether ammonia is transferred through this channelin GatCAB by visualizing ammonia, neutron diffraction studies are indispensable.Here, GatCAB crystals were grown to approximate dimensions of2.8  0.8  0.8 mm (a volume of 1.8 mm3) with the aid of a polymer usingmicroseeding and macroseeding processes. Monochromatic neutron diffractiondata were collected using the neutron single-crystal diffractometer BIODIFF atthe Heinz Maier-Leibnitz Zentrum, Germany. The GatCAB crystals belonged tospace group P212121, with unit-cell parameters a = 74.6, b = 94.5, c = 182.5 A ˚ andwith one GatCAB complex (molecular mass 119 kDa) in the asymmetric unit.This study represented a challenge in current neutron diffraction technology.
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:30839294
%U <Go to ISI:>//WOS:000460520900009
%R 10.1107/S2053230X19000220
%U https://juser.fz-juelich.de/record/872853