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Instruments / Technical Area	Publication Details	Published
Krios I-Titan Krios I at Diamond	Electron cryo-microscopy reveals the structure of the archaeal thread filament Matthew C. Gaines , Michail N. Isupov , Shamphavi Sivabalasarma , Risat U. I. Haque , Mathew Mclaren , Clara L. Mollat , Patrick Tripp , Alexander Neuhaus , Vicki A. M. Gold , Sonja-Verena Albers , Bertram Daum Nature Communications 13 DOI: 10.1038/s41467-022-34652-4 Open Access Show Abstract ▼ Abstract: Pili are filamentous surface extensions that play roles in bacterial and archaeal cellular processes such as adhesion, biofilm formation, motility, cell-cell communication, DNA uptake and horizontal gene transfer. The model archaeaon Sulfolobus acidocaldarius assembles three filaments of the type-IV pilus superfamily (archaella, archaeal adhesion pili and UV-inducible pili), as well as a so-far uncharacterised fourth filament, named “thread”. Here, we report on the cryo-EM structure of the archaeal thread. The filament is highly glycosylated and consists of subunits of the protein Saci_0406, arranged in a head-to-tail manner. Saci_0406 displays structural similarity, but low sequence homology, to bacterial type-I pilins. Thread subunits are interconnected via donor strand complementation, a feature reminiscent of bacterial chaperone-usher pili. However, despite these similarities in overall architecture, archaeal threads appear to have evolved independently and are likely assembled by a distinct mechanism.	Dec 2022
I02-Macromolecular Crystallography I24-Microfocus Macromolecular Crystallography	Identification and characterization of a heterotrimeric archaeal DNA polymerase holoenzyme Jiangyu Yan , Thomas R. Beattie , Adriana L. Rojas , Kelly Schermerhorn , Tamzin Gristwood , Jonathan C. Trinidad , Sonja V. Albers , Pietro Roversi , Andrew F. Gardner , Nicola G. A. Abrescia , Stephen D. Bell Nature Communications 8 DOI: 10.1038/ncomms15075 Diamond Proposal Number(s): [9063, 10130] Open Access Show Abstract ▼ Abstract: Since their initial characterization over 30 years ago, it has been believed that the archaeal B-family DNA polymerases are single-subunit enzymes. This contrasts with the multi-subunit B-family replicative polymerases of eukaryotes. Here we reveal that the highly studied PolB1 from Sulfolobus solfataricus exists as a heterotrimeric complex in cell extracts. Two small subunits, PBP1 and PBP2, associate with distinct surfaces of the larger catalytic subunit and influence the enzymatic properties of the DNA polymerase. Thus, multi-subunit replicative DNA polymerase holoenzymes are present in all three domains of life. We reveal the architecture of the assembly by a combination of cross-linking coupled with mass spectrometry, X-ray crystallography and single-particle electron microscopy. The small subunits stabilize the holoenzyme assembly and the acidic tail of one small subunit mitigates the ability of the enzyme to perform strand-displacement synthesis, with important implications for lagging strand DNA synthesis.	May 2017
I03-Macromolecular Crystallography	Structure and mechanism of the CMR complex for CRISPR-mediated antiviral immunity Jing Zhang , Christophe Rouillon , Melina Kerou , Judith Reeks , Kim Brugger , Shirley Graham , Julia Reimann , Giuseppe Cannone , Huanting Liu , Sonja-Verena Albers , James H. Naismith , Laura Spagnolo , Malcolm f. White Molecular Cell DOI: 10.1016/j.molcel.2011.12.013 PMID: 22227115 Show Abstract ▼ Abstract: The prokaryotic clusters of regularly interspaced palindromic repeats (CRISPR) system utilizes genomically encoded CRISPR RNA (crRNA), derived from invading viruses and incorporated into ribonucleoprotein complexes with CRISPR-associated (CAS) proteins, to target and degrade viral DNA or RNA on subsequent infection. RNA is targeted by the CMR complex. In Sulfolobus solfataricus, this complex is composed of seven CAS protein subunits (Cmr1-7) and carries a diverse “payload” of targeting crRNA. The crystal structure of Cmr7 and low-resolution structure of the complex are presented. S. solfataricus CMR cleaves RNA targets in an endonucleolytic reaction at UA dinucleotides. This activity is dependent on the 8 nt repeat-derived 5? sequence in the crRNA, but not on the presence of a protospacer-associated motif (PAM) in the target. Both target and guide RNAs can be cleaved, although a single molecule of guide RNA can support the degradation of multiple targets.	Jan 2012

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