Factors correlating with significant differences between X-ray structures of myoglobin

Conformational differences between myoglobin structures are studied. Most structural differences in whale myoglobin beyond the uncertainty threshold can be correlated with a few specific structural factors. There are always exceptions and a search for additional factors is needed. The results might have serious implications for biological insights from conformational differences.

Structure of crenactin, an archaeal actin homologue active at 90°C

The crystal structure of the heat-stable archaeal actin, crenactin, is revealed and atomic-level details are presented and compared with those of eukaryotic actin and bacterial MreB.