Creativity and commerce: Michael Klinger and new film history

The crisis in film studies and history concerning their legitimacy and objectives has provoked a reinvigoration of scholarly energy in historical enquiry. 'New film history' attempts to address the concerns of historians and film scholars by working self-reflexively with an expanded range of sources and a wider conception of 'film' as a dynamic set of processes rather than a series of texts. The practice of new film history is here exemplified through a detailed case study of the independent British producer Michael Klinger (active 1961-87) with a specific focus on his unsuccessful attempt to produce a war film, Green Beach, based on a memoir of the Dieppe raid (August 1942). This case study demonstrates the importance of analysing the producer's role in understanding the complexities of film-making, the continual struggle to balance the competing demands of creativity and commerce. In addition, its subject matter - an undercover raid and a Jewish hero - disturbed the dominant myths concerning the Second World War, creating what turned out to be intractable ideological as well as financial problems. The paper concludes that the concerns of film historians need to engage with broader cultural and social histories. © 2010 Taylor & Francis

An analysis and evaluation of the WeFold collaborative for protein structure prediction and its pipelines in CASP11 and CASP12

Every two years groups worldwide participate in the Critical Assessment of Protein Structure Prediction (CASP) experiment to blindly test the strengths and weaknesses of their computational methods. CASP has significantly advanced the field but many hurdles still remain, which may require new ideas and collaborations. In 2012 a web-based effort called WeFold, was initiated to promote collaboration within the CASP community and attract researchers from other fields to contribute new ideas to CASP. Members of the WeFold coopetition (cooperation and competition) participated in CASP as individual teams, but also shared components of their methods to create hybrid pipelines and actively contributed to this effort. We assert that the scale and diversity of integrative prediction pipelines could not have been achieved by any individual lab or even by any collaboration among a few partners. The models contributed by the participating groups and generated by the pipelines are publicly available at the WeFold website providing a wealth of data that remains to be tapped. Here, we analyze the results of the 2014 and 2016 pipelines showing improvements according to the CASP assessment as well as areas that require further adjustments and research

Determining crystal structures through crowdsourcing and coursework

We show here that computer game players can build high-quality crystal structures. Introduction of a new feature into the computer game Foldit allows players to build and real-space refine structures into electron density maps. To assess the usefulness of this feature, we held a crystallographic model-building competition between trained crystallographers, undergraduate students, Foldit players and automatic model-building algorithms. After removal of disordered residues, a team of Foldit players achieved the most accurate structure. Analysing the target protein of the competition, YPL067C, uncovered a new family of histidine triad proteins apparently involved in the prevention of amyloid toxicity. From this study, we conclude that crystallographers can utilize crowdsourcing to interpret electron density information and to produce structure solutions of the highest quality

Protein design by citizen scientists

Thesis (Ph.D.)--University of Washington, 2019Proteins are a class of molecule best known for their tendency to fold into well-defined 3-dimensional structures. The structure of a protein is determined by the sequence of amino acid units that make up the protein. Our understanding of the sequence-structure relationship has recently reached the point that we can design new proteins de novo (i.e. without reference to existing protein sequences). However, this understanding is only partially encoded in protein design software, which still requires a user with considerable expertise in protein engineering. Here, I use citizen science to identify and resolve limitations of protein design software, by crowdsourcing protein design tasks to non-experts playing the computer game Foldit. Using the output of Foldit players as feedback, I iteratively trialed and improved protein design software to the point that non-experts can now use the software to successfully design proteins from scratch. This work reveals implicit assumptions of expert protein engineers, corrects errors in the Rosetta protein structure energy function, and shows how citizen science can be used to improve a scientific model

Creating Custom Foldit Puzzles for Teaching Biochemistry

The computer game Foldit is currently widely used as a biology and biochemistry teaching aid. Herein, we introduce a new feature of Foldit called “custom contests” that allows educators to create puzzles that fit their curriculum. The effectiveness of the custom contests is demonstrated by the use of five distinct custom contests in an upper‐level biochemistry class. The new custom contest feature can be implemented in classes ranging from middle school to graduate school to enable educators to best complement their current curriculum. © 2019 International Union of Biochemistry and Molecular Biology, 47(2): 133–139, 2019

Building de novo cryo-electron microscopy structures collaboratively with citizen scientists

International audienceWith the rapid improvement of cryo-electron microscopy (cryo-EM) resolution, new computational tools are needed to assist and improve upon atomic model building and refinement options. This communication demonstrates that microscopists can now collaborate with the players of the computer game Foldit to generate high-quality de novo structural models. This development could greatly speed the generation of excellent cryo-EM structures when used in addition to current methods