Fig. 2
From: Enzyme intermediates captured “on the fly” by mix-and-inject serial crystallography
Overview of BlaC as determined using 10 × 10 × 3 μm3 sized crystals in the shard form at 500 ms after mixing with 300 mM CEF at room temperature. The mFo-DFc SA-omit electron density is shown for the covalently bound intermediate E-CFO* in green (contour level 2.5 σ). Electron density of an additional, stacked ceftriaxone molecule near the active site is shown in dark green (contour level 2 σ). a The BlaC subunits A–D displayed in blue, yellow, green and light yellow, respectively. Amino acid residues that interact with the stacked CEF are labeled. Panels b and c show enlarged views of the active sites of subunits B and D, respectively. Arg-126 and Tyr-127 with which the respective stacked CEF molecules interact are shown. Some important distances are also displayed (stacked molecules are also observed at the other time delays in the shard crystal form but not in the needles)