3V82: Thaumatin By Lb Based Hanging Drop Vapour Diffusion After 1.81 Mgy X- Ray Dose At Esrf Id29 Beamline (best Case)

A state-of-the-art review of the role of the Langmuir-Blodgett nanotemplate on protein crystal structures is here presented. Crystals grown by nanostructured template appear more radiation resistant than the classical ones, even in the presence of a third-generation highly focused beam at the European Synchrotron Radiation Facility. The electron density maps and the changes in parameters such as total diffractive power, B-factor, and pairwise R-factor have been discussed. Protein crystals, grown by the Langmuir-Blodgett nanotemplate-based method, proved to be more radiation resistant compared to crystals grown by the classical hanging drop method in terms of both global and specific damage.
PDB ID: 3V82Download
MMDB ID: 104723
PDB Deposition Date: 2011/12/22
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 2.3  Å
Source Organism:
Similar Structures:
Biological Unit for 3V82: monomeric; determined by author and by software (PISA)
Molecular Components in 3V82
Label Count Molecule
Protein (1 molecule)
Thaumatin I
Molecule annotation
Chemicals (4 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB