S
S.J. Remington
Researcher at University of Oregon
Publications - 46
Citations - 6044
S.J. Remington is an academic researcher from University of Oregon. The author has contributed to research in topics: Citrate synthase & Protein structure. The author has an hindex of 32, co-authored 46 publications receiving 5832 citations. Previous affiliations of S.J. Remington include Max Planck Society.
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Journal ArticleDOI
Structure of the complex of l-benzylsuccinate with wheat serine carboxypeptidase ii at 2.0-a resolution
TL;DR: The structure of the complex of L-benzylsuccinate bound to wheat serine carboxypeptidase II has been analyzed and suggests a novel enzymatic mechanism, involving substrate-assisted catalysis, that might account for the low pH optimum of peptidase activity unique to this family of serine proteinases.
Book ChapterDOI
Experience with various techniques for the refinement of protein structures
TL;DR: This chapter reviews the experiences with the refinement techniques Real Space Refinement (RLSP), COnstrained-REstrained Least-Squares (CORELS) and EREF.
Journal ArticleDOI
Crystallization and preliminary X-ray studies of human erythrocyte acylpeptide hydrolase.
TL;DR: Crystals of acylpeptide hydrolase suitable for structure determination have been obtained and the search for suitable heavy-atom derivatives is underway.
Journal ArticleDOI
Crystallization and preliminary X-ray studies of Escherichia coli glycerol kinase.
TL;DR: Escherichia coli glycerol kinase, a major regulatory enzyme which catalyzes the reversible MgATP-dependent phosphorylation of Glycerol has been crystallized by the hanging drop vapor diffusion method at room temperature and appears to be suitable for X-ray crystallographic studies.
Journal ArticleDOI
Atomic coordinates for T4 phage lysozyme
TL;DR: Atomic coordinates are presented for the lysozyme from T4 bacteriophage based on a resolution electron density map based on two isomorphous heavy-atom derivatives, interpreted in terms of the known amino acid sequence, and adjusted to have stereochemically acceptable bond lengths and angles.