High-impact research with PILATUS and EIGER data

So far in 2017, EIGER and PILATUS contributed 15 structures to 7 Nature, Science and Cell publications.

7 Molecular mechanism for the regulation of yeast separase by securin.
Authors Luo S, Tong L.
Citation Nature. 2017 Feb 9;542(7640):255-9.
PDB codes 5U1T
Equipment PILATUS3 @ APS BL 24-ID-C
Summary The serine protease separase is important for sister chromatid segregation during mitosis. Its activity is suppressed by the regulator securin. The first crystal structure of a separase–securin complex defines interactions critical for inhibition and the stability of the complex.
6 DNA-PKcs structure suggests an allosteric mechanism modulating DNA double-strand break repair.
Authors Sibanda BL, Chirgadze DY, Ascher DB, Blundell TL.
Citation Science. 2017 Feb 3;355(6324):520-524.
PDB codes 5LUQ
Equipment PILATUS 6M @ ESRF BLs ID23-1, ID29
Summary Repair of DNA double-strand breaks is important to avoid cell death or cancer. The structure of the DNA-dependent kinase catalytic subunit bound to a C-terminal peptide of Ku80, a recruitment factor, suggests an allosteric mechanism of kinase activation. Competition between Ku80 and the tumor suppressor BRCA1 selects different pathways of DNA repair.
5 Structural basis for nutrient acquisition by dominant members of the human gut microbiota.
Authors Glenwright AJ, Pothula KR, Bhamidimarri SP, Chorev DS, Baslé A, Firbank SJ, Zheng H, Robinson CV, Winterhalter M, Kleinekathöfer U, Bolam DN, van den Berg B.
Citation Nature. 2017 Jan 19;541(7637):407-11.
PDB codes 5FQ3 5FQ4 5FQ6 5FQ7 5FQ8 5T4Y 5T3R
Equipment PILATUS3 6M @ DLS BLs I03, I24; PILATUS 6M @ DLS BL I04
Summary Microorganisms in the human gut play important roles in health and nutrition. They feed on dietary glycans that humans cannot metabolize. Here, the crystal structures of two bacterial glycan transporters give insight into how nutrients are imported across the outer membrane of human gut microbes.
4 Pyocyanin degradation by a tautomerizing demethylase inhibits Pseudomonas aeruginosa biofilms.
Authors Costa KC, Glasser NR, Conway SJ, Newman DK.
Citation Science. 2017 Jan 13;355(6321):170-173.
PDB codes 5K21
Equipment PILATUS 6M @ SSRL BL 12-2
Summary Pyocyanin is the best-studied of several redox-active metabolites of the opportunistic pathogen Pseudomonas aeruginosa that is responsible for biofilm formation and virulence. Pyocyanin oxidase, which disrupts biofilm formation, represents a therapeutic lead for difficult bacterial infections.
3 Two distant catalytic sites are responsible for C2c2 RNase activities.
Authors Liu L, Li X, Wang J, Wang M, Chen P, Yin M, Li J, Sheng G, Wang Y.
Citation Cell. 2017 Jan 12;168(1-2):121-134.e12.
PDB codes 5WTJ
Equipment PILATUS3 @ SSRF BL 19U1
Summary C2c2 is a CRISPR nuclease with two RNase activities, cutting its RNA target and processing CRISPR RNA. The crystal structure provides insight into the mechanism of the two RNase activities and establishes a framework for engineering of C2c2 as an RNA editing tool.
2 A supramolecular assembly mediates lentiviral DNA integration.
Authors Ballandras-Colas A, Maskell DP, Serrao E, Locke J, Swuec P, Jónsson SR, Kotecha A, Cook NJ, Pye VE, Taylor IA, Andrésdóttir V, Engelman AN, Costa A, Cherepanov P.
Citation Science. 2017 Jan 6;355(6320):93-95.
PDB codes 5LLJ 5T3A
Equipment PILATUS 6M @ DLS BL I04; PILATUS 2M @ DLS BL I04-1
Summary Lentiviruses like HIV-1 integrate their DNA into the host genome. Viral integrase is thus a major drug target. Using electron cryomicroscopy and X-ray crystallography, this study shows how integrase binds viral DNA to form a complex called the intasome that contains 16 integrase molecules in eight distinct conformations.
1 Structural basis of an essential interaction between influenza polymerase and Pol II CTD.
Authors Lukarska M, Fournier G, Pflug A, Resa-Infante P, Reich S, Naffakh N, Cusack S.
Citation Nature. 2017 Jan 5;541(7635):117-21.
PDB codes 5M3H 5M3J
Equipment PILATUS 6M @ ESRF BLs ID23-1, ID29
Summary Influenze polymerase is a heterotrimer that binds to promoters of each of the eight viral genome segments and performs transcription and replication. The crystal structure of bat influenza A polymerase bound to a peptide mimic of host RNA polymerase II C-terminal domain shows the fine-tuning required for efficient viral transcription and identifies targets for potential antiviral drugs.