F
Fabrice Gorrec
Researcher at Laboratory of Molecular Biology
Publications - 19
Citations - 1401
Fabrice Gorrec is an academic researcher from Laboratory of Molecular Biology. The author has contributed to research in topics: Protein crystallization & Crystallization. The author has an hindex of 11, co-authored 18 publications receiving 1171 citations. Previous affiliations of Fabrice Gorrec include GlaxoSmithKline.
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The MORPHEUS II protein crystallization screen
TL;DR: MORPHEUS II is a 96-condition initial crystallization screen formulated de novo that incorporates reagents selected from the Protein Data Bank to yield crystals that are not observed in traditional conditions.
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Crystal Structures and Nuclear Magnetic Resonance Studies of the Apo Form of the c-MYC:MAX bHLHZip Complex Reveal a Helical Basic Region in the Absence of DNA.
Susan Sammak,Najoua Hamdani,Fabrice Gorrec,Mark D. Allen,Stefan M.V. Freund,Mark Bycroft,Giovanna Zinzalla +6 more
TL;DR: Detailed structural analysis of the apo form of the c-MYC:MAX complex with no artificial linker is carried out, which provides both insight into the mechanism of DNA binding and structural information to aid in the development of MYC inhibitors.
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Pi sampling: a methodical and flexible approach to initial macromolecular crystallization screening
TL;DR: Pi sampling, derived from the incomplete factorial approach, is an effort to maximize the diversity of macromolecular crystallization conditions and to facilitate the preparation of 96-condition initial screens.
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Protein crystallization screens developed at the MRC Laboratory of Molecular Biology.
TL;DR: Three types of initial screens and an optimization screen for protein crystallization are presented, composed of maximally diverse sets of conditions, which were selected to formulate the LMB sparse matrix.
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The current approach to initial crystallization screening of proteins is under-sampled.
TL;DR: Forty-seven main reagents included in a large set of macromolecular crystallization conditions are shown to have a similar impact overall on the yield of crystal structures.