Infection of the human stomach by *Helicobacter pylori* remains a worldwide

problem and greatly contributes to peptic ulcer disease and gastric cancer.

Without active

intervention approximately 50% of the world population will

continue to be infected with this gastric pathogen. Current eradication,

called triple therapy, entails a proton-pump inhibitor and two broadband

antibiotics, however resistance to either clarithromycin or metronidazole

is greater than 25% and rising. Therefore, there is an urgent need for a

targeted, high-specificity eradication drug.

Gastric infection by

*H. pylori* depends on the expression of a nickel-dependent urease in the

cytoplasm of the bacteria. Here, we report the 2.0 Å resolution structure

of the 1.1 MDa urease in complex with a novel inhibitor by cryo-electron

microscopy and compare it to a b

-

mercaptoethanol-inhibited structure at 2.5

Å resolution. The structural information is of sufficient detail to aid in

the development of inhibitors with high specificity and affinity.

About ALBA II Colloquium

The series ALBA II Colloquium, addressed to the scientific user's community of synchrotron radiation, is aimed at inspiring and promoting fruitful ideas and information exchange about the future development of ALBA II facility.