issue contents

ISSN: 2053-230X

January 2021 issue

Highlighted illustration

Cover illustration: Structural analysis of the chicken FANCM-MHF complex [Ito & Nishino (2021), Acta Cryst. F77, 1-7]. FANCM is involved in eukaryotic DNA-damage recognition and activates the Fanconi anemia (FA) pathway through complex formation. MHF is one of the FANCM-associating components and contains a histone-fold DNA-binding domain. Loss of the FANCM-MHF interaction compromises the activation of the FA pathway, resulting in chromosomal instability. Thus, formation of the FANCM-MHF complex is important for function, but until now its nature has remained largely elusive.

research communications

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Three crystals of MHF and its complex with FANCM were obtained, and structural analysis revealed not only their structures but the unexpected release of FANCM from MHF. The biochemical stability of the FANCM–MHF complex was analyzed and it was found that an oxidative environment and organic solvent promote the aggregation and dissociation of the complex.

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Protein crystallization and X-ray data collection of the N-terminal Solanaceae domain of the Sw-5b NLR immune receptor are described.

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The crystal structure of human V-1 in the apo form was determined at 2.3 Å resolution. The results demonstrate that V-1 is a constitutively active inhibitor of actin-capping protein.

methods communications

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Yeast surface display was applied to a library of hematopoietic progenitor kinase 1 (HPK1) kinase domain variants in order to select those with an improved expression level and solubility. The HPK1 variant with the most improved properties contained two mutations and crystallized readily in complex with several small-molecule inhibitors.


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An improved, fully automated protein crystallization and monitoring system, PXS2, can perform crystallization using smaller protein samples than the previous version. In addition, PXS2 can be used for membrane-protein crystallization using the bicelle and LCP methods.
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