issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

November 2009 issue

Highlighted illustration

Cover illustration: The 1.9 Å structure of the branched-chain amino-acid transaminase (IlvE) from Mycobacterium tuberculosis (Tremblay & Blanchard , p. 1071).

structural communications


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The structure of the branched-chain amino-acid transaminase (IlvE) from M. tuberculosis has been resolved at 1.9 Å resolution. The structure, together with sequence conservation, identifies residues that are likely to be responsible for substrate specificity with mechanistic and potential therapeutic relevance.

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The crystal structure of the adenylation domain of NAD+-dependent DNA ligase from Staphylococcus aureus reveals a narrow `C2 tunnel' for potential use in inhibitor design.

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The structure of N-terminally truncated DR2204, a Nudix hydrolase, is presented at 2.0–Å resolution.

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The 1.45 Å structure of E. coli N-acetyl-D-neuraminic acid lyase in complex with pyruvate in space group P212121 is reported from new low-salt crystallization conditions that will facilitate soaking experiments with substrates and inhibitors.

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The crystal structures of the human NAIP BIR2 and cIAP2 BIR3 domains have been determined. Both BIR domains harbors an amino-terminal tetrapeptide in its peptide-binding groove.

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This report shows that the tertiary structure of rabbit FGF-1 is essentially identical to that of human FGF-1, with four surface mutations (140-amino-acid form). Biophysical data indicate that rabbit FGF-1 is less thermostable than human FGF-1 and has a slower association rate with the FGF-1 receptor. Mitogenic assays indicate that rabbit FGF-1 is tenfold less potent than human FGF-1; however, rabbit FGF-1 exhibits greater heparin stimulation such that its mitogenic activity in the presence of heparin is essentially indistinguishable from that of human FGF-1.

crystallization communications



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Sedoheptulose-7-phosphate isomerase (GmhA) from B. pseudomallei is one of the targets of antibiotic adjuvants for melioidosis. In this study, GmhA has been cloned, expressed, purified and crystallized.

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Diffraction-quality crystals of an atypical two-cysteine peroxiredoxin (SAOUHSC_01822) from S. aureus NCTC 8325 have been obtained. The cloning, overexpression, purification, crystallization and preliminary X-ray diffraction analysis of the protein are reported.

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Overexpression, purification, crystallization and preliminary X-ray diffraction analysis of the nucleoside diphosphate kinase b from Leishmania major are reported. The crystals belonged to the trigonal space group P3221 and diffracted to 2.18 Å resolution.

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A hexagonal crystal of free methionine-(R)-sulfoxide reductase from S. aureus has been obtained using ammonium sulfate as a precipitant.

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AmtR is a rare example of a member of the TetR family of bacterial transcription regulators that is not regulated by a small-molecule effector but by interaction with a protein named GlnK. Wild-type and SeMet-substituted AmtR have been produced and crystallized and preliminary electron-density maps have been obtained to 3.0 Å resolution.

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The bacterial PPM phosphatase RsbX from B. subtilis was expressed in E. coli, purified and crystallized. The crystal belonged to space group P1 and diffracted to 1.06 Å resolution.

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The proliferating cell nuclear antigen (PCNA) from the eurypsychrophilic archaeon M. burtonii DSM 6242 has been cloned, overproduced, purified and crystallized. Crystals were deemed to be suitable for X-ray analysis and structure determination to 2.40 Å resolution.

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A solvent-mediated crystal contact in fibroblast growth factor-1 was subjected to mutagenesis to improve crystal growth. The results indicate that improved growth was achieved upon elimination of the solvent-mediated interface and introduction of direct crystal contacts.

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Clostridium thermocellum D-­ribose-5-phosphate isomerase has been purified and crystallized in order to determine its three-dimensional structure and thus to elucidate its enzymatic reaction mechanism and understand its substrate specificity.

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Conjugated polyketone reductase C2 from C. parapsilosis IFO 0708 was expressed, purified and crystallized by the sitting-drop vapour-diffusion method. The crystal belonged to space group P212121 and diffracted X-rays to 1.7 Å resolution.

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The head and predicted galectin-like domains of porcine adenovirus NADC-1 isolate fibre have been independently crystallized. Diffraction data have been obtained to 3.2 Å resolution for the head-domain crystals and to 1.9 Å resolution for the galectin-like domain crystals.

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The protein complex of bifunctional isocitrate dehydrogenase kinase/phosphatase with its substrate, isocitrate dehydrogenase, has been crystallized for structural analysis. A complete data set was collected from the complex crystal and processed to 2.9 Å resolution.

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In order to validate the hypothesis of a shared recognition mode for the CMV immunodominant NLV-HLA-A2 epitope by specific high-avidity T-cell clones, a second public TCR, RA15, in complex with NLV-HLA-A2 was overexpressed, purified and crystallized. Preliminary diffraction data obtained at 4.7 Å resolution and a molecular-replacement solution suggest an overall similar docking mode for RA15 TCR on NLV-HLA-A2 compared with the public RA14 TCR, for which the structure has previously been solved.

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The invertase from Schwanniomyces occidentalis has been expressed in Saccharomyces cerevisiae, purified and crystallized. The wild-type enzyme was also purified and crystallized and diffraction data were collected to 2.9 Å resolution.

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Mutations in the human AAA+ protein p97 cause a disease in humans called IBMPFD. How these mutations affect the structure and function of p97 is unknown. Here, the crystallization of three disease-related mutants of p97 in the presence of ATPγS are reported.

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Gallate dioxygenase (DesB) from Sphingobium sp. SYK-6, which belongs to the type II extradiol dioxygenase family, was purified and crystallized in two different crystal forms, which were subjected to X-ray analysis.

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Crystals of complexes of the T. cruzi dihydrofolate reductase-thymidylate synthase enzyme with three antifolates in two space groups have been obtained that diffracted to 2.1–2.8 Å resolution. The antifolates used for cocrystallization were dihydrotriazine-based and quinazoline-based antifolates.


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The breakage-reunion domain of M. tuberculosis DNA gyrase was crystallized using the hanging-drop vapour-diffusion method. One of the four crystal forms obtained belonged to space group C2 and diffraction data were collected to a resolution of 2.7 Å.

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Crystallization conditions have been determined for an extracellular portion of the Ser/Thr kinase Stk1 from the human pathogen S. aureus that contains three PASTA subunits. Synchrotron data have been collected to a resolution of 2.9 Å. Phasing is in progress.

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The preliminary X-ray analysis of β-glucosidase (BglI) from K. marxianus, which belongs to glycoside hydrolase family 3, is described.

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The expression, purification, crystallization and preliminary diffraction analysis of an archaeal-type phosphoenolpyruvate carboxylase are described. Complete highly redundant X-ray data have been measured from a crystal diffracting to 3.13 Å resolution.

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γ-Carboxymucolactone decarboxylase from the thermophilic archaeon S. solfataricus was crystallized. Diffraction to 2.40 Å resolution was obtained from a flash-cooled crystal using synchrotron radiation.
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