A low-resolution low-temperature neutron diffraction study of myoglobin.

Diffraction data to 5 A resolution were collected on a myoglobin crystal at 80, 130, 180 and 240 K. The linear coefficient of thermal expansion for myoglobin was determined to be 45 x 10(-6) K(-1), based on the measured expansion of the unit-cell parameters. The nature of the hydration layers surrounding the protein in the crystal is described in terms of a shell solvent model, which was used to calculate the coefficient of thermal expansion in reasonable agreement with the measured value.

Crystal structure of the DpnM DNA adenine methyltransferase from the DpnII restriction system of streptococcus pneumoniae bound to S-adenosylmethionine.

Background: . Methyltransferases (Mtases) catalyze the transfer of methyl groups from S-adenosylmethionine (AdoMet) to a variety of small molecular and macromolecular substrates. These enzymes contain a characteristic alpha/beta structural fold.

Myoglobin solvent structure at different temperatures.

The structure of the solvent surrounding myoglobin crystals has been analyzed using neutron diffraction data, and the results indicate that the water around the protein is not disordered, but rather lies in well-defined hydration shells. We have analyzed the structure of the solvent surrounding the protein by collecting neutron diffraction data at four different temperatures, namely, 80, 130, 180, and 240K. Relative Wilson Statistics applied to low resolution data showed evidence of a phase transition in the region of 180K.

On the structure of the nickel/iron/sulfur center of the carbon monoxide dehydrogenase from Rhodospirillum rubrum: an x-ray absorption spectroscopy study.

The nickel/iron/sulfur center of the carbon monoxide dehydrogenase (carbon monoxide:(acceptor)oxidoreductase; EC 1.2.99.