Tek Narsingh Malla

University of Wisconsin-Milwaukee

ABSTRACT

Structural enzymology is now possible at X-ray free electron lasers (XFELs) using mix-and-inject serial crystallography (MISC) technology. In time resolved (TR) MISC, reaction in enzymatic crystals is triggered by mixing with a substrate, and the resulting structural changes are probed by X-ray pulses. We have been studying Mycobacterium tuberculosis β-lactamase (BlaC) as a model system. Previous experiments using ceftriaxone (CEF) as substrate solution demonstrated the robust case for routine (TR) MISC at XFELs. Time resolution, however, has been diffusion limited due to large CEF molecule that has to diffuse into enzyme crystals. With recent experience of binding study with sulbactam (SUB), a 3 times smaller molecule than CEF, we planned to push the time resolution of the MISC to the limit. Besides, SUB, in addition, is an inhibitor that irreversibly binds to BlaC. Here we present the results of lowest time resolution ever achieved with MISC, and the enzymatic reaction of BlaC with SUB. 

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Email: tmalla@uwm.edu