Structure of the Tpp49Aa1 pesticidal protein elucidated from natural crystals using MHz-SFX.

The proteins Tpp49Aa1 and Cry48Aa1 can together act as a toxin toward the mosquito and have potential use in biocontrol. Given that proteins with sequence homology to the individual proteins can have activity alone against other insect species, the structure of Tpp49Aa1 was solved in order to understand this protein more fully and inform the design of improved biopesticides. Tpp49Aa1 is naturally expressed as a crystalline inclusion within the host bacterium, and MHz serial femtosecond crystallography using the novel nanofocus option at an X-ray free electron laser allowed rapid and high-quality data collection to determine the structure of Tpp49Aa1 at 1.

The role of glycoconjugates as receptors for insecticidal proteins.

Bacillus thuringiensis (Bt) proteins are an environmentally safe and effective alternative to chemical pesticides and have been used as biopesticides, with great commercial success, for over 50 years. Global agricultural production is predicted to require a 70% increase until 2050 to provide for an increasing population. In addition to agriculture, Bt proteins are utilized to control human vectors of disease-namely mosquitoes-which account for >700 000 deaths annually.

The Crystal Structure of Tpp80Aa1 and Its Interaction with Galactose-Containing Glycolipids.

Tpp80Aa1 from is a Toxin_10 family protein (Tpp) with reported action against mosquitoes. Here, we demonstrate an expanded target range, showing Tpp80Aa1 is also active against the larvae of and mosquitoes. We report the first crystal structure of Tpp80Aa1 at a resolution of 1.

The Crystal Structure of HblL.

The Hbl toxin is a three-component haemolytic complex produced by strains and implicated as a cause of diarrhoea in food poisoning. While the structure of the HblB component of this toxin is known, the structures of the other components are unresolved. Here, we describe the expression of the recombinant HblL component and the elucidation of its structure to 1.