Crystal Structure and Mutational Analysis of Isomalto-dextranase, a Member of Glycoside Hydrolase Family 27

Structural and biochemical characterization of novel bacterial α-galactosidases belonging to glycoside hydrolase family 31

(2015) Takatsugu Miyazaki et al.   BIOCHEMICAL JOURNAL

Structural Elucidation of the Cyclization Mechanism of α-1,6-Glucan byBacillus circulansT-3040 Cycloisomaltooligosaccharide Glucanotransferase

(2014) Nobuhiro Suzuki et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Structural and Biochemical Analyses of Glycoside Hydrolase Family 26 β-Mannanase from a Symbiotic Protist of the TermiteReticulitermes speratus

(2014) Hikaru Tsukagoshi et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Experimental and Modeling Studies of an Unusual Water-Filled Pore Structure with Possible Mechanistic Implications in Family 48 Cellulases

(2014) Mo Chen et al.   JOURNAL OF PHYSICAL CHEMISTRY B

Structure–specificity relationships in Abp, a GH27 β-L-arabinopyranosidase fromGeobacillus stearothermophilusT6

(2014) Shifra Lansky et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Advances in understanding the molecular basis of plant cell wall polysaccharide recognition by carbohydrate-binding modules

(2013) Harry J Gilbert et al.   CURRENT OPINION IN STRUCTURAL BIOLOGY

The carbohydrate-active enzymes database (CAZy) in 2013

(2013) Vincent Lombard et al.   NUCLEIC ACIDS RESEARCH

Crystal structure of a lactosucrose-producing enzyme, Arthrobacter sp. K-1 β-fructofuranosidase

(2012) Takashi Tonozuka et al.   ENZYME AND MICROBIAL TECHNOLOGY

CAVER 3.0: A Tool for the Analysis of Transport Pathways in Dynamic Protein Structures

(2012) Eva Chovancova et al.   PLoS Computational Biology

Overview of theCCP4 suite and current developments

(2011) Martyn D. Winn et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

LigPlot+: Multiple Ligand–Protein Interaction Diagrams for Drug Discovery

(2011) Roman A. Laskowski et al.   Journal of Chemical Information and Modeling

Features and development ofCoot

(2010) P. Emsley et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Signature Active Site Architectures Illuminate the Molecular Basis for Ligand Specificity in Family 35 Carbohydrate Binding Module,

(2010) Márcia A. S. Correia et al.   BIOCHEMISTRY

Dali server: conservation mapping in 3D

(2010) Liisa Holm et al.   NUCLEIC ACIDS RESEARCH

Decision-making in structure solution using Bayesian estimates of map quality: thePHENIX AutoSolwizard

(2009) Thomas C. Terwilliger et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Molecular replacement withMOLREP

(2009) Alexei Vagin et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

MolProbity: all-atom structure validation for macromolecular crystallography

(2009) Vincent B. Chen et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Catalytic Mechanism of Human α-Galactosidase

(2009) Abigail I. Guce et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

A β-l-Arabinopyranosidase fromStreptomyces avermitilisIs a Novel Member of Glycoside Hydrolase Family 27

(2009) Hitomi Ichinose et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Bacterial Extracellular Polysaccharides Involved in Biofilm Formation

(2009) Barbara Vu et al.   MOLECULES

Evidence that family 35 carbohydrate binding modules display conserved specificity but divergent function

(2009) C. Montanier et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Complete genome sequence of Catenulispora acidiphila type strain (ID 139908T)

(2009) Alex Copeland et al.   Standards in Genomic Sciences

Plant glycosyl hydrolases and biofuels: a natural marriage

(2008) G LOPEZCASADO et al.   CURRENT OPINION IN PLANT BIOLOGY

Substrate Recognition Mechanism of α-1,6-Glucosidic Linkage Hydrolyzing Enzyme, Dextran Glucosidase from Streptococcus mutans

(2008) Hironori Hondoh et al.   JOURNAL OF MOLECULAR BIOLOGY

Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7

(2008) Gerrit Langer et al.   Nature Protocols