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	<title>serial femtosecond crystallography &#8211; BIOENGINEER.ORG</title>
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		<title>X-ray Lasers Catch Penicillin-Making Enzyme in the Act, Revealing Surprise Intermediates</title>
		<link>https://bioengineer.org/x-ray-lasers-catch-penicillin-making-enzyme-in-the-act-revealing-surprise-intermediates/</link>
		
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		<pubDate>Fri, 09 Oct 2026 12:51:12 +0000</pubDate>
				<category><![CDATA[Chemistry]]></category>
		<category><![CDATA[active-site water]]></category>
		<category><![CDATA[enzyme mechanism]]></category>
		<category><![CDATA[iron oxygenase]]></category>
		<category><![CDATA[isopenicillin N synthase]]></category>
		<category><![CDATA[penicillin biosynthesis]]></category>
		<category><![CDATA[protein dynamics]]></category>
		<category><![CDATA[serial femtosecond crystallography]]></category>
		<category><![CDATA[structural biology]]></category>
		<category><![CDATA[thioaldehyde intermediate]]></category>
		<category><![CDATA[X-ray emission spectroscopy]]></category>
		<category><![CDATA[X-ray free-electron laser]]></category>
		<category><![CDATA[β-lactam antibiotics]]></category>
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					<description><![CDATA[Time-resolved X-ray free-electron laser crystallography has captured previously unseen intermediates in the enzyme that forges the penicillin ring system, revealing an unexpected release of the substrate sulfur from iron and critical roles for active-site water molecules.]]></description>
		
		
		
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