4EKH

Final Thaumatin Structure for Radiation Damage Experiment at 100 K

Summary for 4EKH

• Entry DOI: 10.2210/pdb4ekh/pdb
• Related: 4EK0 4EKA 4EKB 4EKO 4EKT 4EL2 4EL3 4EL7 4ELA
• Descriptor: Thaumatin-1, L(+)-TARTARIC ACID (3 entities in total)
• Functional Keywords: sweet protein, radiation damage, plant protein
• Biological source: Thaumatococcus daniellii (katemfe)
• Cellular location: Cytoplasmic vesicle: P02883
• Total number of polymer chains: 1
• Total formula weight: 22393.21

Authors

Warkentin, M.,Badeau, R.,Hopkins, J.B.,Thorne, R.E. (deposition date: 2012-04-09, release date: 2012-08-29, Last modification date: 2024-11-27)

Primary citation

Warkentin, M.,Badeau, R.,Hopkins, J.B.,Thorne, R.E.
Spatial distribution of radiation damage to crystalline proteins at 25-300 K.
Acta Crystallogr.,Sect.D, 68:1108-1117, 2012

PubMed Abstract: The spatial distribution of radiation damage (assayed by increases in atomic B factors) to thaumatin and urease crystals at temperatures ranging from 25 to 300 K is reported. The nature of the damage changes dramatically at approximately 180 K. Above this temperature the role of solvent diffusion is apparent in thaumatin crystals, as solvent-exposed turns and loops are especially sensitive. In urease, a flap covering the active site is the most sensitive part of the molecule and nearby loops show enhanced sensitivity. Below 180 K sensitivity is correlated with poor local packing, especially in thaumatin. At all temperatures, the component of the damage that is spatially uniform within the unit cell accounts for more than half of the total increase in the atomic B factors and correlates with changes in mosaicity. This component may arise from lattice-level, rather than local, disorder. The effects of primary structure on radiation sensitivity are small compared with those of tertiary structure, local packing, solvent accessibility and crystal contacts.

PubMed: 22948911
DOI: 10.1107/S0907444912021361

Experimental method

X-RAY DIFFRACTION (1.75 Å)