@article {8678,
	title = {Exploring Advances in Single Particle CryoEM with Apoferritin: from Blobs to True Atomic Resolution [National Cryo-EM Facility, BLiSC (INT)]},
	journal = {The International Journal of Biochemistry \& Cell Biology},
	year = {2024},
	month = {02/2024},
	type = {Review},
	abstract = {<p><span style="color: rgb(31, 31, 31); font-family: ElsevierGulliver, Georgia, \&quot;Times New Roman\&quot;, Times, STIXGeneral, \&quot;Cambria Math\&quot;, \&quot;Lucida Sans Unicode\&quot;, \&quot;Microsoft Sans Serif\&quot;, \&quot;Segoe UI Symbol\&quot;, \&quot;Arial Unicode MS\&quot;, serif; font-size: 16px;">Deciphering the three-dimensional structures of macromolecules is of paramount importance for gaining insights into their functions and roles in human health and disease. Single particle cryoEM has emerged as a powerful technique that enables direct visualization of macromolecules and their complexes, and through subsequent averaging, achieve near atomic-level resolution. A major breakthrough was recently achieved with the determination of the apoferritin structure at true atomic resolution. In this review, we discuss the latest technological innovations across the entire single-particle workflow, which have been instrumental in driving and expanding the resolution revolution and in transforming cryoEM as a mainstream technique in structural biology. We illustrate these advancements using apoferritin as an example that has served as an excellent benchmark sample for assessing emerging technologies. We further explore whether the existing technology can routinely generate atomic structures of dynamic macromolecules that more accurately represent real-world samples, the limitations in the workflow and the current approaches employed to overcome them.</span></p>
},
	doi = {https://doi.org/10.1016/j.biocel.2024.106536},
	url = {https://www.sciencedirect.com/science/article/abs/pii/S135727252400027X},
	author = {Gowtham ThambraRajan Premageetha and Kutti R. Vinothkumar and Sucharita Bose}
}
@article {1160,
	title = {Molecular basis for metabolite channeling in a ring opening enzyme of the phenylacetate degradation pathway [National Cryo-Electron Microscopy Facility (INT)]},
	journal = {Nature Communications},
	volume = {10},
	year = {2019},
	month = {09, 2019},
	type = {Article},
	chapter = {4127},
	abstract = {Substrate channeling is a mechanism for the internal transfer of hydrophobic, unstable or toxic intermediates from the active site of one enzyme to another. Such transfer has previously been described to be mediated by a hydrophobic tunnel, the use of electrostatic highways or pivoting and by conformational changes. The enzyme PaaZ is used by many bacteria to degrade environmental pollutants. PaaZ is a bifunctional enzyme that catalyzes the ring opening of oxepin-CoA and converts it to 3-oxo-5,6-dehydrosuberyl-CoA. Here we report the structures of PaaZ determined by electron cryomicroscopy with and without bound ligands. The structures reveal that three domain-swapped dimers of the enzyme form a trilobed structure. A combination of small-angle X-ray scattering (SAXS), computational studies, mutagenesis and microbial growth experiments suggests that the key intermediate is transferred from one active site to the other by a mechanism of electrostatic pivoting of the CoA moiety, mediated by a set of conserved positively charged residues.},
	keywords = {Bacterial structural biology, Cryoelectron microscopy, Multienzyme complexes},
	author = {Nitish Sathyanarayanan and Giuseppe Cannone and Lokesh Gakhar and Nainesh Katagihallimath and Ramanathan Sowdhamini and Subramanian Ramaswamy and Kutti R. Vinothkumar}
}
