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Eric de La Fortelle

Researcher at Laboratory of Molecular Biology

Publications -  8
Citations -  3023

Eric de La Fortelle is an academic researcher from Laboratory of Molecular Biology. The author has contributed to research in topics: AP endonuclease & Binding site. The author has an hindex of 7, co-authored 8 publications receiving 2991 citations.

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Book ChapterDOI

[27] Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods

TL;DR: This chapter discusses the maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement (MIR) and multiwavelength anomalous diffraction (MAD) and its extension to probability distributions incorporating anomalousdiffraction effects, as well as measurement error and nonisomorphism.
Journal ArticleDOI

Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs.

TL;DR: Crystal structures suggest that the seven Sm proteins could form a closed ring and the snRNAs may be bound in the positively charged central hole.
Journal ArticleDOI

The crystal structure of the human DNA repair endonuclease HAP1 suggests the recognition of extra‐helical deoxyribose at DNA abasic sites

TL;DR: The HAP1 structure suggests a mechanism for AP site binding which involves the recognition of the deoxyribose moiety in an extra‐helical conformation, rather than a ‘flipped‐out’ base opposite the AP site.
Journal ArticleDOI

Crystal structure of the anti-fungal target N-myristoyl transferase.

TL;DR: The groove and pocket are the sites of substrate binding and the floor of the pocket is the catalytic center of N-myristoyl transferase, which has a novel α/β fold which shows internal twofold symmetry, which may be a result of gene duplication.
Journal ArticleDOI

Crystal structure of a fungal elicitor secreted by Phytophthora cryptogea, a member of a novel class of plant necrotic proteins

TL;DR: The determination of the crystal structure of a member of the elicitin family may make it possible to separate the activity that causes leaf necrosis from that inducing systemic acquired resistance to pathogens, making it feasible to engineer a non-toxic elicitin that only elicits plant defences.