issue contents

ISSN: 2053-230X

October 2019 issue

Highlighted illustration

Cover illustration: A 22-base-pair RNA helix with mismatched pyrimidine base pairs [Montemayor et al. (2019), Acta Cryst. F75, 652-656]. The helix contains two symmetry-related CUG sequences: a triplet-repeat motif implicated in myotonic dystrophy type 1. The CUG repeat contains a U-U mismatch sandwiched between Watson-Crick pairs. Additionally, the center of the helix contains a dimerized UUCG motif with tandem pyrimidine (U-C/C-U) mismatches flanked by U-G wobble pairs. This region of the structure is significantly different from previously observed structures that share the same sequence and neighboring base pairs. The tandem pyrimidine mismatches are unusual and show that pyrimidine-rich regions of RNA have a high degree of structural diversity.

research communications

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The crystal structure of the Lactobacillus helveticus PepX enzyme was determined at 2.0 Å resolution, providing the second structural example of a peptidase from the S15 family of the SC clan.

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The crystal structure of the Fab region of a neutralizing fully human antibody against granulocyte-macrophage colony-stimulating factor is reported.

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Bovine β-lactoglobulin was crystallized at pH 3.8 from 3 M NaCl in a unique crystal form with apparent P6322 symmetry. The hexagonal prismatic crystal in fact belonged to space group C2221, a subgroup of P6322, with three molecules in the asymmetric unit and exhibited an unusual type of twinning. The structure was solved by molecular replacement and refined to an R factor of 0.23.

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Rv0100 is an essential acyl carrier protein for the pathogenesis and growth of Mycobacterium tuberculosis. Using Mycobacterium smegmatis as a host, Rv0100 was successfully cloned, purified and crystallized, and the crystals diffracted to 1.9 Å resolution.

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The structure of a 22-base-pair RNA helix with mismatched pyrimidine base pairs is reported. The pyrimidine mismatches are unusual and display sheared, cross-strand stacking geometries that locally constrict the helical width.

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Pneumococcal adherence and virulence factor A (PavA) plays a key role in the adhesion of Streptococcus pneumoniae to host tissues. Here, the crystal structure of the N-terminal domain of PavA is presented, which reveals structural differences from its homologs.
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