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4N4Z

Trypanosoma brucei procathepsin B structure solved by Serial Microcrystallography using synchrotron radiation

Summary for 4N4Z
Entry DOI10.2210/pdb4n4z/pdb
Related4HWY
DescriptorCysteine peptidase C (CPC), 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
Functional Keywordspapain fold, hydrolase, propeptide, glycosylation
Biological sourceTrypanosoma brucei brucei
Total number of polymer chains1
Total formula weight38270.63
Authors
Primary citationGati, C.,Bourenkov, G.,Klinge, M.,Rehders, D.,Stellato, F.,Oberthur, D.,Yefanov, O.,Sommer, B.P.,Mogk, S.,Duszenko, M.,Betzel, C.,Schneider, T.R.,Chapman, H.N.,Redecke, L.
Serial crystallography on in vivo grown microcrystals using synchrotron radiation.
IUCrJ, 1:87-94, 2014
Cited by
PubMed Abstract: Crystal structure determinations of biological macromolecules are limited by the availability of sufficiently sized crystals and by the fact that crystal quality deteriorates during data collection owing to radiation damage. Exploiting a micrometre-sized X-ray beam, high-precision diffractometry and shutterless data acquisition with a pixel-array detector, a strategy for collecting data from many micrometre-sized crystals presented to an X-ray beam in a vitrified suspension is demonstrated. By combining diffraction data from 80 Trypanosoma brucei procathepsin B crystals with an average volume of 9 µm(3), a complete data set to 3.0 Å resolution has been assembled. The data allowed the refinement of a structural model that is consistent with that previously obtained using free-electron laser radiation, providing mutual validation. Further improvements of the serial synchrotron crystallography technique and its combination with serial femtosecond crystallography are discussed that may allow the determination of high-resolution structures of micrometre-sized crystals.
PubMed: 25075324
DOI: 10.1107/S2052252513033939
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.3 Å)
Structure validation

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