Publications by authors named "Doris Zoric"
Article Synopsis
- * Researchers used time-resolved serial femtosecond crystallography to examine how the CO’s active site reacts when carbon monoxide is rapidly removed from its heme structure.
- * Findings reveal that the CO binds more stably to copper through interactions with a water molecule, explaining the longer duration of the Cu-CO complex and the enzyme's high affinity for oxygen.
Serial femtosecond crystallography was initially developed for room-temperature X-ray diffraction studies of macromolecules at X-ray free electron lasers. When combined with tools that initiate biological reactions within microcrystals, time-resolved serial crystallography allows the study of structural changes that occur during an enzyme catalytic reaction. Serial synchrotron X-ray crystallography (SSX), which extends serial crystallography methods to synchrotron radiation sources, is expanding the scientific community using serial diffraction methods.
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