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Six structures of bovine pancreatic ribonuclease at six pH values have been refined and analyzed. A comparative analysis of the six models and some biological implications are discussed.

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The structure of recombinant RNase Sa from 1.0 Å spacing synchrotron data collected at cryogenic temperature shows two alternative conformations of the main chain in two loops which contain active-site residues. This feature was not observed in the structure refined against room-temperature data at 1.2 Å resolution.

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The structure of the endoglucanase A from Clostridium thermocellum CelA has been re-solved by three-wavelength MAD.
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