PDBsum entry 3v82

Plant protein

PDB id: 3v82

Contents

Protein chain

207 a.a.

Ligands

GOL ×4

Waters ×186

PDB id:

3v82

Name:

Plant protein

Title:

Thaumatin by lb based hanging drop vapour diffusion after 1.81 mgy x- ray dose at esrf id29 beamline (best case)

Structure:

Thaumatin i. Chain: a

Source:

Thaumatococcus daniellii. Katemfe. Organism_taxid: 4621

Resolution:

2.30Å R-factor: 0.183 R-free: 0.237

Authors:

L.Belmonte,D.Scudieri,S.Tripathi,E.Pechkova,C.Nicolini

Key ref:

L.Belmonte et al. (2012). Langmuir-Blodgett nanotemplate and radiation resistance in protein crystals: state of the art. Crit Rev Eukaryot Gene Expr, 22, 219-232. PubMed id: 23140163

Date:

22-Dec-11 Release date: 07-Nov-12

Protein chain

P02883  (THM1_THADA) -  Thaumatin I from Thaumatococcus daniellii

Seq: 235 a.a.

Struc: 207 a.a.

Crit Rev Eukaryot Gene Expr 22:219-232 (2012)

PubMed id: 23140163

Langmuir-Blodgett nanotemplate and radiation resistance in protein crystals: state of the art.

L.Belmonte, E.Pechkova, S.Tripathi, D.Scudieri, C.Nicolini.

ABSTRACT

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.