Back to Search
Start Over
Natively inhibited Trypanosoma brucei cathepsin B structure determined by using an X-ray laser
- Source :
- Science
- Publication Year :
- 2013
-
Abstract
- Diffraction Before Destruction A bottleneck in x-ray crystallography is the growth of well-ordered crystals large enough to obtain high-resolution diffraction data within an exposure that limits radiation damage. Serial femtosecond crystallography promises to overcome these constraints by using short intense pulses that out-run radiation damage. A stream of crystals is flowed across the free-electron beam and for each pulse, diffraction data is recorded from a single crystal before it is destroyed. Redecke et al. (p. 227 , published online 29 November; see the Perspective by Helliwell ) used this technique to determine the structure of an enzyme from Trypanosoma brucei , the parasite that causes sleeping sickness, from micron-sized crystals grown within insect cells. The structure shows how this enzyme, which is involved in degradation of host proteins, is natively inhibited prior to activation, which could help in the development of parasite-specific inhibitors.
- Subjects :
- Models, Molecular
Glycosylation
Protein Conformation
Molecular Sequence Data
Trypanosoma brucei brucei
Protozoan Proteins
Biology
Trypanosoma brucei
Spodoptera
Crystallography, X-Ray
Cathepsin B
In vivo
Catalytic Domain
Sf9 Cells
Animals
Angstrom
Amino Acid Sequence
Host protein
Enzyme Precursors
Multidisciplinary
X-Rays
biology.organism_classification
Protozoan parasite
Cysteine protease
Biochemistry
Fatal disease
Crystallization
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Journal :
- Science
- Accession number :
- edsair.doi.dedup.....6ffe3f3ebf77275dc22b4ca432e54163