5LH3
High dose Thaumatin - 0-40 ms.
Summary for 5LH3
Entry DOI | 10.2210/pdb5lh3/pdb |
Descriptor | Thaumatin-1, L(+)-TARTARIC ACID (3 entities in total) |
Functional Keywords | multicrystal, room-temperature, thaumatin, plant protein |
Biological source | Thaumatococcus daniellii (Katemfe) |
Total number of polymer chains | 1 |
Total formula weight | 22527.23 |
Authors | Schubert, R.,Kapis, S.,Heymann, M.,Giquel, Y.,Bourenkov, G.,Schneider, T.,Betzel, C.,Perbandt, M. (deposition date: 2016-07-08, release date: 2016-11-09, Last modification date: 2024-10-16) |
Primary citation | Schubert, R.,Kapis, S.,Gicquel, Y.,Bourenkov, G.,Schneider, T.R.,Heymann, M.,Betzel, C.,Perbandt, M. A multicrystal diffraction data-collection approach for studying structural dynamics with millisecond temporal resolution. IUCrJ, 3:393-401, 2016 Cited by PubMed Abstract: Many biochemical processes take place on timescales ranging from femto-seconds to seconds. Accordingly, any time-resolved experiment must be matched to the speed of the structural changes of interest. Therefore, the timescale of interest defines the requirements of the X-ray source, instrumentation and data-collection strategy. In this study, a minimalistic approach for crystallization is presented that requires only a few microlitres of sample solution containing a few hundred crystals. It is demonstrated that complete diffraction data sets, merged from multiple crystals, can be recorded within only a few minutes of beamtime and allow high-resolution structural information of high quality to be obtained with a temporal resolution of 40 ms. Global and site-specific radiation damage can be avoided by limiting the maximal dose per crystal to 400 kGy. Moreover, analysis of the data collected at higher doses allows the time-resolved observation of site-specific radiation damage. Therefore, our approach is well suited to observe structural changes and possibly enzymatic reactions in the low-millisecond regime. PubMed: 27840678DOI: 10.1107/S2052252516016304 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.64 Å) |
Structure validation
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