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Florian Hollfelder

Researcher at University of Cambridge

Publications -  208
Citations -  10356

Florian Hollfelder is an academic researcher from University of Cambridge. The author has contributed to research in topics: Biology & Chemistry. The author has an hindex of 49, co-authored 173 publications receiving 8704 citations. Previous affiliations of Florian Hollfelder include École Polytechnique Fédérale de Lausanne & Central Queensland University.

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Journal ArticleDOI

Ultra-High-Throughput Absorbance-Activated Droplet Sorting for Enzyme Screening at Kilohertz Frequencies

TL;DR: In this article , the authors improved absorbance-activated droplet sorting (AADS) to reach kHz sorting speeds in an order of magnitude increase over previous designs with close-to-ideal sorting accuracy.
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A Titratable Cell Lysis-on-Demand System for Droplet-Compartmentalized Ultrahigh-Throughput Screening in Functional Metagenomics and Directed Evolution.

TL;DR: In this article, a titratable lysis-on-demand (LoD) system was proposed to control the rate of cell lysis in Escherichia coli by adjusting the externally added inducer concentration.
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Controlled Ligand Exchange Between Ruthenium Organometallic Cofactor Precursors and a Naïve Protein Scaffold Generates Artificial Metalloenzymes Catalysing Transfer Hydrogenation.

TL;DR: In this paper, RuII (η6 -arene)(bipyridine) complexes designed to facilitate the displacement of functionalised bipyridines were systematically tested and ligand exchange was used to unmask catalytic activity.
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Just (protein) engineering

TL;DR: His group is based in the Biochemistry Department at Cambridge and its research centres around quantitative and mechanistic questions at the chemistry/ biology interface, involving lowand highthroughput approaches.
Book ChapterDOI

USER Friendly DNA Recombination (USERec): Gene Library Construction Requiring Minimal Sequence Homology

TL;DR: The greatly reduced sequence constraints of this method facilitate directional assembly of gene fragments for applications such as exon or domain shuffling, loop grafting, reassembly of natural modular biosynthetic assembly lines, and rearrangement of structurally (but not sequence) homologous proteins.