issue contents

Journal logoBIOLOGICAL
CRYSTALLOGRAPHY
ISSN: 1399-0047

September 2012 issue

Highlighted illustration

Cover illustration: Lid-loop motion in the active site of alginate lyase A1-III. The lid loop (residues 64-85) moves from an open to a closed form to make interactions with a bound substrate (spheres) and a catalytic Tyr residue (p. 1207).

research papers


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The crystal structure of MoSub1, a Sub1/PC4 orthologue from rice blast fungus, has two novel features N-terminal and C-terminal to the DNA-binding domain. It has a similar dimer interface and DNA-binding region to PC4 and the protein binds single-stranded DNA tightly.

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Experimental errors in macromolecular crystallography are underestimated as they do not account for the contribution of crystal-to-crystal variations.

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The crystal structures of the far-red fluorescent proteins eqFP650 and eqFP670 have been solved at 1.8 and 1.6 Å resolution, respectively. This permitted identification of the structural elements responsible for the bathochromic shift in both considered far-red fluorescent proteins.


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Dose-dependent atomic B factors are used to determine the average spatial distribution of radiation damage to crystalline thaumatin and urease.

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The values of atomic shifts in unrestrained refinement can hint at alternative conformations.

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The 2.4 Å crystal structure of the protein augmenter of liver regeneration (hsALR) containing a 14-residue histidine purification tag has been determined by Cd-SAD. The structure reveals a tetramer (two hsALR homodimers) bridged by a novel Cd2Cl4O6 cluster that produces a crystal packing environment that can better accommodate the N-terminal purification tag.

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The BAM complex is comprised of an integral β-barrel outer membrane protein BamA and four accessory lipoproteins BamB, BamC, BamD and BamE. Here, the crystal structure of BamB is reported.

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Three crystal structures of a lipoprotein (Bmlp7) of unknown function, a member of the 30 kDa lipoprotein family from mulberry silkworm (B. mori L.) haemolymph, have been determined. The haemolymph-isolated protein was identified through successful sequence assignment according to electron-density maps at 1.33 Å resolution.

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A method for experimental phasing by segmenting a large data set into sub-data sets for radiation-damage-induced phasing is presented.

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The structure of a tetrameric sponge galectin suggests a basis for glutamate receptor potentiation.

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Structures of FtsZ from S. aureus in apo, GDP-bound and PC190723-complex forms are reported; FtsZ undergoes distinct conformational changes. These structural features are discussed and related to the crucial functions of FtsZ.

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P99 cephalosporinase is a class C β-lactamase that is responsible in part for the widespread bacterial resistance to β-­lactam antibiotics. Here, the X-ray crystal structure of the apo Asn152Gly mutant of P99 has been determined to 1.95 Å resolution.

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The structure of Giardia prolyl-tRNA synthetase cocrystallized with proline and ATP shows evidence for half-of-the-sites activity, leading to a corresponding mixture of reaction substrates and product (prolyl-AMP) in the two active sites of the dimer.

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A joint X-ray/neutron structure of D-xylose isomerase in complex with the inhibitor sorbitol was determined at room temperature at an acidic pH of 5.9. Protonation of the O5 O atom of the sugar was directly observed in the nuclear density maps. Under acidic conditions sorbitol gains a water-mediated interaction with the enzyme active site, which may explain the increased potency of the inhibitor at low pH.

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The structures of apo and holo mutants of alginate lyase A1-III revealed a large open/closed conformational change of lid loop. The closed lid loop is involved both in the binding of substrate and catalysis of the enzyme.

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Determination of the orientation of the enterovirus 71 virions in the crystal required the calculation of a locked rotation function that included only icosahedral threefold and fivefold symmetry axes. Otherwise, misleading high rotation-function values were produced by accidental alignment of icosahedral and crystallographic twofold axes.

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An updated picture of the ligand sets and copper–ligand atom bond lengths in proteins is presented.

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The crystal structure of thymidylate synthase from E. faecalis was obtained as a native complex with 5-formyltetrahydrofolate (5-FTHF). The structure supports the role of 5-FTHF, which is naturally present in the bacterial cell, as a storage form of the folate metabolite and as an enzyme regulator.

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The crystal structure of the 11.14 kDa orphan ORF 1382 from Archaeoglobus fulgidus (AF1382) has been determined by sulfur SAD phasing using data collected from a moderately diffracting crystal and 1.9 Å synchrotron X-rays.

short communications


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The surface of proteins can be charged with zinc ions and the anomalous signals from these zinc ions can be used for structure determination of proteins.
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