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This journal provides immediate access to some articles. Volume 63(Pt 1); January 1, 2007 Protein Structure Communications Effects of the magnesium and chloride ions and shikimate on the structure of shikimate kinase from Mycobacterium tuberculosis
The crystal structure of MtSK in complex with ADP shows conformational changes caused by the absence of the shikimate molecule, and the effect of chloride ions on the nucleotide binding site, and the crystal structure of MtSK in absence of magnesium shows its effect on the shikimate binding site. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 January 1; 63(Pt 1): 1–6. Published online 2006 December 16. doi: 10.1107/S1744309106046823.PMCID: PMC2330112 Structure of the catalytic domain of the hyperthermophilic chitinase from Pyrococcus furiosus
The crystal structure of the catalytic domain of a chitinase from P. furiosus is reported. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 January 1; 63(Pt 1): 7–11. Published online 2006 December 16. doi: 10.1107/S1744309106051773.PMCID: PMC2330115 Crystallization Communications Purification, crystallization and preliminary X-ray analysis of the BseCI DNA methyltransferase from Bacillus stearothermophilus in complex with its cognate DNA The DNA methyltransferase M.BseCI from B. stearothermophilus was crystallized as a complex with its cognate DNA. Crystals belong to space group P6 and diffract to 2.5 Å resolution at a synchrotron source. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 January 1; 63(Pt 1): 12–14. Published online 2006 December 16. doi: 10.1107/S1744309106051530.PMCID: PMC2330102 Purification, crystallization and preliminary crystallographic analysis of archaeal 6-pyruvoyl tetrahydrobiopterin synthase homologue PH0634 from Pyrococcus horikoshii OT3 An archaeal 6-pyruvoyl tetrahydrobiopterin synthase homologue from P. horikoshii OT3 was overexpressed as native and selenomethionine-substituted protein, purified and crystallized. The native and selenomethionine-derivative crystals are isomorphous and diffract X-rays to 2.1 and 2.9 Å resolution, respectively. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 January 1; 63(Pt 1): 15–17. Published online 2006 December 16. doi: 10.1107/S1744309106051578.PMCID: PMC2330099 Expression, purification and preliminary crystallographic studies on the catalytic region of the nonreceptor tyrosine kinase Fes The catalytic domain of human Fes tyrosine kinase has been cloned, expressed, purified and crystallized. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 January 1; 63(Pt 1): 18–20. Published online 2006 December 16. doi: 10.1107/S1744309106051682.PMCID: PMC2330100 Purification, crystallization and preliminary crystallographic characterization of the caspase-recruitment domain of human Nod1 The caspase-recruitment domain of the cytosolic pathogen receptor Nod1 was crystallized. X-ray diffraction data were collected to 1.9 Å resolution. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 January 1; 63(Pt 1): 21–23. Published online 2006 December 16. doi: 10.1107/S1744309106051955.PMCID: PMC2330101 Preliminary crystallographic analysis of avian infectious bronchitis virus main protease The avian infectious bronchitis virus main protease has been crystallized; crystals diffract to 2.7 Å resolution. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 January 1; 63(Pt 1): 24–26. Published online 2006 December 16. doi: 10.1107/S1744309106052341.PMCID: PMC2330114 Crystallization and preliminary crystallographic analysis of molybdenum-cofactor biosynthesis protein C from Thermus thermophilus
The molybdenum-cofactor biosynthesis protein C from T. thermophilus has been crystallized in two different space groups, P21 and R32; the crystals diffracted to 1.9 and 1.75 Å resolution, respectively. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 January 1; 63(Pt 1): 27–29. Published online 2006 December 16. doi: 10.1107/S1744309106052560.PMCID: PMC2330104 Preliminary X-ray analysis of XC5848, a hypothetical ORFan protein with an Sm-like motif from Xanthomonas campestris
A conserved hypothetical protein Se-XC5848 from X. campestris pv. campestris has been overexpressed in E. coli, purified and crystallized. Crystals obtained from the purified recombinant protein diffracted to a resolution of 1.68 Å. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 January 1; 63(Pt 1): 30–33. Published online 2006 December 16. doi: 10.1107/S1744309106052730.PMCID: PMC2330107 Preliminary structural studies of the transcriptional regulator CmeR from Campylobacter jejuni
The transcriptional regulator CmeR from C. jejuni has been purified and crystallized and X-ray diffraction data have been collected to a resolution of 2.2 Å. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 January 1; 63(Pt 1): 34–36. Published online 2006 December 16. doi: 10.1107/S1744309106053127.PMCID: PMC2330109 Preliminary X-ray diffraction analysis of YcdB from Escherichia coli: a novel haem-containing and Tat-secreted periplasmic protein with a potential role in iron transport The crystallization and structure determination of the apo form of a novel haem-containing Tat substrate, YcdB from E. coli, has been solved to 2.0 Å resolution. The preliminary structure shows similarity to other haem-dependent peroxidases, despite low sequence homology. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 January 1; 63(Pt 1): 37–41. Published online 2006 December 22. doi: 10.1107/S174430910604509X.PMCID: PMC2330106 Preliminary time-of-flight neutron diffraction study on diisopropyl fluorophosphatase (DFPase) from Loligo vulgaris
Diisopropyl fluorophosphatase (DFPase) effectively hydrolyzes a number of organophosphorus nerve agents, including sarin, cyclohexylsarin, soman and tabun. Neutron diffraction data have been collected from DFPase crystals to 2.2 Å resolution in an effort to gain further insight into the mechanism of this enzyme. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 January 1; 63(Pt 1): 42–45. Published online 2006 December 22. doi: 10.1107/S1744309106052924.PMCID: PMC2330113 Crystallization and preliminary X-ray diffraction analysis of an Escherichia coli tRNAGly acceptor-stem microhelix In order to investigate the identity elements of the E. coli tRNAGly/GlyRS class II system, a tRNAGly acceptor-stem microhelix was crystallized and a data set was collected to 2.0 Å resolution using synchrotron radiation. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 January 1; 63(Pt 1): 46–48. Published online 2006 December 22. doi: 10.1107/S1744309106052870.PMCID: PMC2330105 Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tails of adhesion molecules CD43 and PSGL-1 The radixin FERM domain has been crystallized in complex with CD43 and PSGL-1 peptides. Diffraction data sets were collected from the complexes to 2.9 and 2.8 Å resolution, respectively. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 January 1; 63(Pt 1): 49–51. Published online 2006 December 22. doi: 10.1107/S1744309106054145.PMCID: PMC2330108 Exploration of triple-helical fragments: crystallization and preliminary X-ray diffraction of d(TGGCCTTAAGG) The crystallization and X-ray data collection of the undecamer d(TGGCCTTAAGG) are reported. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 January 1; 63(Pt 1): 52–55. Published online 2006 December 22. doi: 10.1107/S1744309106054522.PMCID: PMC2330110 Purification, crystallization and preliminary crystallographic analysis of the putative thiamine-biosynthesis protein PH1313 from Pyrococcus horikoshii OT3 The putative thiamine-biosynthesis protein PH1313 from P. horikoshii OT3 was overexpressed, purified and crystallized. The crystals belong to space group P212121 and diffract X-rays to 1.9 Å resolution. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 January 1; 63(Pt 1): 56–58. Published online 2006 December 22. doi: 10.1107/S1744309106054509.PMCID: PMC2330111 Addenda and Errata Crystallization and preliminary X-ray diffraction analysis of two N-terminal fragments of the DNA-cleavage domain of topoisomerase IV from Staphylococcus aureus. Corrigendum A corrigendum to the paper by Carr et al. (2006), Acta Cryst. F62, 1164–1167. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 January 1; 63(Pt 1): 59. Published online 2006 December 22. doi: 10.1107/S1744309106054650.PMCID: PMC2330103 Corrects:Crystallization and preliminary X-ray diffraction analysis of two N-terminal fragments of the DNA-cleavage domain of topoisomerase IV from Staphylococcus aureus
. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 November 1; 62(Pt 11): 1164–1167. | ||