issue contents

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983

September 2025 issue

Highlighted illustration

Cover illustration: The XFBLD-Platform is a crystallographic fragment-screening platform at Shanghai Synchrotron Radiation Facility [Huang et al. (2025), Acta Cryst. D81, 482–491]. The XFBLD-Viewer component illustrated here streamlines the identification of droplets containing well-formed crystals and enables precise spatial targeting for compound addition in directed soaking experiments.

research papers


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This study presents the crystal structure of human β2-microglobulin (β2M) complexed with the monoclonal antibody BBM.1, revealing critical interactions involving key epitope residues. These structural insights validate prior biochemical findings and provide a foundational basis for the development of precise therapeutic approaches targeting β2M in various diseases.

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A crystallographic fragment-screening platform, referred to as the XFBLD-Platform, developed at Shanghai Synchrotron Radiation Facility accelerates fragment-based lead discovery through an integrated high-throughput workflow for structure-based drug development.


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Variants HNL16, HNL40 and HNL71 of hydroxynitrile lyase from Hevea brasiliensis contain 16, 40 and 71 mutations, respectively, to make increasingly larger regions surrounding the active site identical in sequence to the esterase SABP2. X-ray structures of HNL40 and HNL71 reveal changes to the oxyanion hole and a new tunnel, which may contribute to their efficient esterase activity.

obituaries


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