Structure of a circularly permuted phosphoglycerate kinase.

The crystallographic structure of a circularly permuted form of yeast PGK, 72p yPGK, has been determined to a resolution of 2.3 A by molecular replacement. In this engineered protein, the C- and N-terminal residues of the wild-type protein are directly connected by a peptide bond and new N- and C-terminal residues are located within the N-terminal domain.

Structural and functional properties of mutant Arg203Pro from yeast phosphoglycerate kinase, as a model of phosphoglycerate kinase-Uppsala.

A pathological variant of human phosphoglycerate kinase, phosphoglycerate kinase-Uppsala, associated with chronic nonspherocytic hemolytic anemia has been found to differ from the normal enzyme by substitution of an arginine at position 206 (corresponding to position 203 in yeast) by a proline. In order to understand the structural and functional consequences of this mutation, the corresponding mutant in yeast phosphoglycerate kinase was constructed. The three-dimensional structure of this mutant was resolved at 2.

Three-dimensional structure of Fab R19.9, a monoclonal murine antibody specific for the p-azobenzenearsonate group.

The crystal structure of Fab R19.9, derived from an anti-p-azobenzenearsonate monoclonal antibody, has been determined and refined to 2.8-A resolution by x-ray crystallographic techniques.

X-ray diffraction studies of an anti-azophenylarsonate antibody and of an antigen-antibody complex.

X-ray crystallographic studies of the Fab fragments of two murine monoclonal antibodies of predefined specificity are under way. Diffracted X-ray intensities of the crystalline native Fab fragment of an anti-azophenylarsonate antibody and of three heavy atom derivatives have been measured to a resolution of 3.5 A.

Crystallization of the fab fragments of monoclonal anti-p-azophenylarsonate antibodies and their complexes with haptens.

We report on the preparation, crystallization, and preliminary x-ray crystallographic study of Fab fragments from monoclonal anti-p-azophenylarsonate antibodies. Several crystalline forms were obtained with the Fab fragment from the R19.9 monoclonal antibody as well as with the complex between the hapten p-aminobenzenearsonic acid and Fab R19.

Preliminary crystallographic study of the Fc fragment of a monoclonal IgG2b murine immunoglobulin.

The Fe fragment of a gamma 2b murine monoclonal anti-p-azophenylarsonate antibody (R19.9, IgG2b, kappa) has been crystallized. The crystals are tetragonal, space group P41 (or P43) with unit cell dimensions: a = b = 134.