ABSTRACT
The N-terminal domain of the regulatory protein TyrR from Escherichia coli forms a dimer in solution and has been purified and crystallized. The crystals belong to space group C2 with unit-cell parameters a = 134.5, b = 72.1, c = 96.7 A, beta = 98.5 degrees. The crystals diffract to 2.8 A. Assuming a molecular weight of 23219 Da, a V(m) of 2.5 A(3) Da(-1) is obtained for two dimers in the asymmetric unit.
Subject(s)
Escherichia coli Proteins , Repressor Proteins/chemistry , Bacterial Proteins/chemistry , Crystallization , Dimerization , Escherichia coli , Peptide Fragments/chemistry , Recombinant Proteins/chemistry , X-Ray DiffractionABSTRACT
Crystals of chloroplast NADP-dependent malate dehydrogenase have been grown both with and without the cofactor NADP present. The enzyme has a molecular weight of 43 kDa per subunit and exists as a dimer in solution. The crystals diffract to 2.8 A and belong to the space group P3221 with cell dimensions a = 148.1, c = 65.5 A.
Subject(s)
Chloroplasts/enzymology , Malate Dehydrogenase/chemistry , Plant Proteins/chemistry , Crystallization , Crystallography, X-Ray , Malate Dehydrogenase (NADP+) , Protein Conformation , TemperatureABSTRACT
The trimeric signal-transduction protein GlnK, from Escherichia coli, has been over-expressed, purified to homogeneity and crystallized. The crystals belong to space group P213 with a = 85.53 A and have two subunits in the asymmetric unit. The complex of GlnK with ATP crystallized in space group P63 with a = 57.45 and c = 54.79 A. These crystals have a single subunit in the asymmetric unit. High-quality diffraction data from crystals of GlnK and the GlnK complex have been collected to 2.0 A.
