issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

September 2018 issue

Highlighted illustration

Cover illustration: The structure of bacterioferritin from Achromobacter at 1.95 Å [Dwivedy et al. (2018), Acta Cryst. F74, 558-566].

research communications


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The structure of the Fc fragment of the NIST reference antibody RM8671 is described in an orthorhombic crystal form. The molecular conformation is compared with those of precedents using a CH3-based reference frame and the pronounced asymmetry is linked to packing interactions.

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The crystal structure of a proteolytic fragment of an MeaB- and MMAA-like GTPase from Mycobacterium smegmatis was determined using the ab initio phasing program ARCIMBOLDO.

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Analysis of the noncrystallographic symmetry of crystals of the C-terminal domain of Burkholderia cenocepacia TssA indicates a quaternary structure of 32 subunits in D16 symmetry.

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The Mycobacterium smegmatis Gre-factor homologue MSMEG_6292 is an RNA polymerase secondary channel-binding protein. To understand its structure and function, it was cloned, expressed, purified and crystallized, and crystallographic diffraction data were collected for both the native protein and a platinum derivative.

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Designed ankyrin-repeat proteins (DARPins) that bind to maltose-binding protein (MBP) with high affinity can facilitate the crystallization of an MBP fusion protein. The use of MBP-specific DARPins increases the probability of obtaining crystals.

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This study reports the structure of bacterioferritin from Achromobacter sp. Dh1f, which was serendipitously crystallized.

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Staphylococcus aureus lipase (SAL), a possible target for anti-staphylococcal drugs, was expressed in Escherichia coli, purified and crystallized. A complete data set to 3.0 Å resolution was corrected and analyzed, suggesting a tetragonal space group (P4122 or P4322, a = b = 131.0, c = 250.6 Å) and four molecules per asymmetric unit.

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The crystallization and X-ray diffraction analysis of the Cqm1 protein, which is known for its role as a receptor for mosquito-larvicidal binary toxin, is reported. The article also highlights the use of differential scanning fluorimetry for screening small-molecule ligands that could contribute to protein crystallization.

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Crystals of different domain constructs of the TssA subunit from Aeromonas hydrophila have been crystallized in forms suitable for X-ray analysis.

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The crystal structure of a non-immunosuppressive cyclic peptide inhibitor bound to its target, human cyclophilin A, is reported.

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The binding of 28 dyes and stains to a dozen crystalline proteins, and to four in particular, was investigated by X-ray crystallography. Crystals of 31 different complexes were studied. Although firmly incorporated into the protein crystals in substantial amounts, the dyes are disordered and are possibly bound in a similar manner to conventional detergents.
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