Neutron crystallographic study of heterotrimeric glutamine amidotransferase CAB

Long Li, Motoyasu Adachi, Jian Yu, Koji Kato, Akira Shinod, Andreas Ostermann, Tobias E. Schrader, Toyoyuki Osea, Min Yao

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)


Heterotrimeric glutamine amidotransferase CAB (GatCAB) possesses an ammonia-self-sufficient mechanism in which ammonia is produced and used in the inner complex by GatA and GatB, respectively. The X-ray structure of GatCAB revealed that the two identified active sites of GatA and GatB are markedly distant, but are connected in the complex by a channel of 30Å in length. In order to clarify whether ammonia is transferred through this channel in GatCAB by visualizing ammonia, neutron diffraction studies are indispensable. Here, GatCAB crystals were grown to approximate dimensions of 2.8 × 0.8 × 0.8mm (a volume of 1.8mm3) with the aid of a polymer using microseeding and macroseeding processes. Monochromatic neutron diffraction data were collected using the neutron single-crystal diffractometer BIODIFF at the Heinz Maier-Leibnitz Zentrum, Germany. The GatCAB crystals belonged to space group P212121, with unit-cell parameters a = 74.6, b = 94.5, c = 182.5Å and with one GatCAB complex (molecular mass 119kDa) in the asymmetric unit. This study represented a challenge in current neutron diffraction technology.

Original languageEnglish
Pages (from-to)193-196
Number of pages4
JournalActa Crystallographica Section F: Structural Biology Communications
Publication statusPublished - 2019
Externally publishedYes


  • GatCAB
  • ammonia channel
  • ammonia-self-sufficient mechanism
  • glutamine amidotransferase CAB
  • neutron diffraction

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics


Dive into the research topics of 'Neutron crystallographic study of heterotrimeric glutamine amidotransferase CAB'. Together they form a unique fingerprint.

Cite this