issue contents

Journal logoBIOLOGICAL
ISSN: 1399-0047

January 2013 issue

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Cover illustration: Cover illustrations from each of the 20 years of Acta Cryst. D.


Acta Cryst. (2013). D69, 1
doi: 10.1107/S0907444912051190

scientific comment

Acta Cryst. (2013). D69, 2-4
doi: 10.1107/S0907444912044794
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The importance of presenting macromolecular structures in unified, standard ways is discussed.

research papers

Acta Cryst. (2013). D69, 5-15
doi: 10.1107/S0907444912039881

Acta Cryst. (2013). D69, 16-23
doi: 10.1107/S0907444912041005
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The S. pyogenes ORF SPy1599, classified into CAZy family GH1, has been shown to display 6-phospho-β-glucosidase activity through a series of kinetics studies on aryl glycosides. The three-dimensional structure has been solved at 2.5 Å resolution from both twinned and untwinned crystal forms.

Acta Cryst. (2013). D69, 24-31
doi: 10.1107/S0907444912041169
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The crystal structure of the metalloprotease Gentlyase is described and compared with the structures of other related thermolysin-like proteases.

Acta Cryst. (2013). D69, 32-43
doi: 10.1107/S0907444912042072
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Crystal structures of 2-amino­phenol 1,6-dioxygenase, an enzyme that represents a minor group of extradiol dioxygenases and that catalyses the ring opening of 2-aminophenol, in complex with the lactone intermediate (4Z,6Z)-3-iminooxepin-2(3H)-one and the product 2-aminomuconic 6-semialdehyde and in complex with the suicide inhibitor 4-nitrocatechol are reported.

Acta Cryst. (2013). D69, 44-51
doi: 10.1107/S0907444912042059
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Biofilm is an extracellular matrix created by many microorganisms, and a major problem in clinical and technical settings. The crystal structure reported here helps elucidate the synthesis of the major component of biofilm produced by Y. pestis and E. coli, and may assist in the development of agents to block it.

Acta Cryst. (2013). D69, 52-62
doi: 10.1107/S0907444912042175
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Two crystal structures of a plant endo-1,3-β-glucanase representing glycoside hydrolase family GH17 in complexes with products of laminarahexose hydrolysis reveal the protein–saccharide interactions at five key binding subsites for the first time. A trisaccharide is bound at subsites −3, −2 and −1 of the nonreducing end (glycon portion) in both structures, and in one structure an extra tetrasaccharide is bound at subsites +1 to +4 of the reducing end (aglycon portion).

Acta Cryst. (2013). D69, 63-73
doi: 10.1107/S0907444912042400
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The crystal structures of an M. thermophila glucuronoyl esterase (StGE2) and of its S213A mutant in the unliganded form and in complex with methyl 4-O-methyl-β-D-glucopyranuronate determined at 1.55, 1.90 and 2.35 Å resolution, respectively, are presented for the first time, disclosing the role of StGE2 as a potential biocatalyst.

Acta Cryst. (2013). D69, 74-81
doi: 10.1107/S0907444912042503
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Polarization-resolved second-harmonic generation microscopy is applied to the identification of multiple crystalline domains within protein-crystal samples.

Acta Cryst. (2013). D69, 82-91
doi: 10.1107/S0907444912042369
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Crystal structures of the AHL-lactonase AidH in complex with substrate and product are reported at high resolution and a catalytic mechanism is proposed for the metal-independent AHL-lactonase.

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Structure of a 20-amino-acid peptide of AHNAK bound asymmetrically to the AnxA2–S100A10A heterotetramer (1:2:2 symmetry) provides insights into the atomic level interactions that govern this membrane-repair scaffolding complex.

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Biogenic amine-binding proteins mediate the anti-inflammatory and antihemostatic activities of blood-feeding insect saliva. The structure of the amine-binding protein from R. prolixus reveals the interaction of biogenic amine ligands with the protein.

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The anticancer agents cisplatin and carboplatin bind to a free histidine in a protein. This crystal structure study at data-collection temperatures of 100 and 300 K examines their relative binding affinities to a histidine side chain and the effect of a high radiation dose on the stability of the subsequent protein–Pt adducts. Cisplatin binding is visible and carboplatin binding is not, indicating stronger binding of cisplatin.

short communications

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NO photodissociation in a tetrameric haemoglobin has been detected via Raman microscopy on protein single crystals during X-ray diffraction data collection at different radiation doses.
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