Centrality evolution of the charged-particle pseudorapidity density over a broad pseudorapidity range in Pb-Pb collisions at root s(NN)=2.76TeV

Peer reviewe

Estudio de un mineral "serpentinico" del departamento Tupungato, Mendoza

Facultad de Ciencias Naturales y Muse

Estudio de un mineral "serpentinico" del departamento Tupungato, Mendoza

Facultad de Ciencias Naturales y Muse

Crystallization and preliminary X-ray diffraction study of a bacterially produced T-cell antigen receptor Vα domain

A recombinant form of the variable domain of the α chain of a murine T- cell receptor specific for the N-terminal nonapeptide of myelin basin protein in association with the major histocompatibility complex class II I-A(u) molecule has been crystallized in a form suitable for X-ray diffraction analysis. This protein was secreted into the periplasmic space of Escherichia coli cells and affinity-purified using a nickel chelate adsorbent. The crystals are orthorhombic, space group P21212, with unit cell dimensions a=97.7 Å, b=79.6 Å, c=30.4 Å and diffract to beyond 2.2 Å resolution. The ability to crystallize a T-cell receptor domain produced in bacteria strongly suggests that the periplasmic space can provide a suitable environment for the correct in vivo folding of this class of antigen recognition molecules.</p

Crystallization and preliminary X-ray diffraction study of the bacterially expressed Fv from the monoclonal anti-lysozyme antibody D1.3 and of its complex with the antigen, lysozyme

The associated heavy (VH) and light (VL) chain variable domains (FV) of the monoclonal anti-lysozyme antibody D1.3, secreted from Escherichia coli, have been crystallized in their antigen-bound and free forms. FvD1.3 gives tetragonal crystals, space group P41212 (or P43212), with a = 90·6 Å, c = 56·4 Å. The FvD1.3-lysozyme complex crystallizes in space group C2, with a = 129·2 Å, b = 60·8 Å, c = 56·9 Å and β = 119·3°. The crystals contain one molecule of Fv or of the Fv-lysozyme complex in their asymmetric units and diffract X-rays to high resolution, making them suitable for X-ray crystallographic studies.</p