In situ structure determination of the ribosomal protein L14 in the large 50S subunit of Escherichia coli

Citation
S. Forthmann et al., In situ structure determination of the ribosomal protein L14 in the large 50S subunit of Escherichia coli, J APPL CRYS, 33(1), 2000, pp. 524-525
Citations number
10
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Physical Chemistry/Chemical Physics
Journal title
JOURNAL OF APPLIED CRYSTALLOGRAPHY
ISSN journal
0021-8898 → ACNP
Volume
33
Issue
1
Year of publication
2000
Part
3
Pages
524 - 525
Database
ISI
SICI code
0021-8898(20000601)33:1<524:ISSDOT>2.0.ZU;2-W
Abstract
Polarized neutron scattering from dynamically polarized nuclear spin target s has become a method of macromolecular structure research. The contrast cr eated by substitution of the hydrogen isotope H-1 by H-2 is increased by al most a factor of three if polarized neutrons are scattered by polarized nuc lear spins in the sample (spin contrast variation). Therefore, this method is also suitable to determine small or weakly contrasted labels. Proteins w ith a mass less than 1 wt.% of the background particle were localized. In t his paper, an extension of our structural model for the 50S subunit by the in situ structure determination of the protein L14 is presented.