scholarly journals Crystallization and preliminary crystallographic study ofFeline infectious peritonitis virusmain protease in complex with an inhibitor

2014 ◽  
Vol 70 (12) ◽  
pp. 1612-1615 ◽  
Author(s):  
Jinshan Wang ◽  
Fenghua Wang ◽  
Yusheng Tan ◽  
Xia Chen ◽  
Qi Zhao ◽  
...  
Keyword(s):  
Antiviral Drug ◽  
Proteolytic Processing ◽  
Genome Replication ◽  
Domestic Cats ◽  
Unit Cell Parameters ◽  
Feline Infectious Peritonitis ◽  
Cell Parameters ◽  
Crystallographic Study ◽  
Main Protease ◽  
Complex Crystals

Feline infectious peritonitis virus(FIPV) causes a lethal systemic granulomatous disease in wild and domestic cats around the world. Currently, no effective vaccines or drugs have been developed against it. As a member of the genusAlphacoronavirus, FIPV encodes two polyprotein precursors required for genome replication and transcription. Each polyprotein undergoes extensive proteolytic processing, resulting in functional subunits. This process is mainly mediated by its genome-encoded main protease, which is an attractive target for antiviral drug design. In this study, the main protease of FIPV in complex with a Michael acceptor-type inhibitor was crystallized. The complex crystals diffracted to 2.5 Å resolution and belonged to space groupI422, with unit-cell parametersa= 112.3,b= 112.3,c= 102.1 Å. There is one molecule per asymmetric unit.

scholarly journals Crystallization and preliminary crystallographic study of human coronavirus NL63 main protease in complex with an inhibitor

2014 ◽  
Vol 70 (8) ◽  
pp. 1068-1071 ◽  
Author(s):  
Fenghua Wang ◽  
Yusheng Tan ◽  
Huiyan Li ◽  
Xia Chen ◽  
Jinshan Wang ◽  
...  
Keyword(s):  
Antiviral Drug ◽  
Proteolytic Processing ◽  
Genome Replication ◽  
Asymmetric Unit ◽  
Unit Cell Parameters ◽  
Human Coronavirus ◽  
Cell Parameters ◽  
Crystallographic Study ◽  
Main Protease ◽  
Complex Crystals

Human coronavirus NL63 mainly infects younger children and causes cough, fever, rhinorrhoea, bronchiolitis and croup. It encodes two polyprotein precursors required for genome replication and transcription. Each polyprotein undergoes extensive proteolytic processing, resulting in functional subunits. This process is mainly mediated by its genome-encoded main protease, which is an attractive target for antiviral drug design. In this study, the main protease of human coronavirus NL63 was crystallized in complex with a Michael acceptor. The complex crystals diffracted to 2.85 Å resolution and belonged to space groupP41212, with unit-cell parametersa=b= 87.2,c= 212.1 Å. Two molecules were identified per asymmetric unit.

scholarly journals Crystallization and preliminary crystallographic study ofPorcine epidemic diarrhea virusmain protease in complex with an inhibitor

2014 ◽  
Vol 70 (12) ◽  
pp. 1608-1611
Author(s):  
Yusheng Tan ◽  
Fenghua Wang ◽  
Xia Chen ◽  
Jinshan Wang ◽  
Qi Zhao ◽  
...  
Keyword(s):  
Porcine Epidemic Diarrhea Virus ◽  
Antiviral Drug ◽  
Proteolytic Processing ◽  
Genome Replication ◽  
Virus Shedding ◽  
Cell Parameters ◽  
Diarrhea Virus ◽  
Main Protease ◽  
Porcine Epidemic Diarrhea ◽  
Complex Crystals

Porcine epidemic diarrhea virus(PEDV) mainly infects neonatal pigs, resulting in significant morbidity and mortality. Owing to problems such as long periods of virus shedding, existing vaccines cannot provide complete protection from PEDV infection. The PEDV genome encodes two polyprotein precursors required for genome replication and transcription. Each polyprotein undergoes extensive proteolytic processing, resulting in functional subunits. This process is mainly mediated by its genome-encoded main protease, which is an attractive target for antiviral drug design. In this study, the main protease ofPorcine epidemic diarrhea virusin complex with a Michael acceptor was crystallized. The complex crystals diffracted to 2.5 Å resolution and belonged to space groupR3, with unit-cell parametersa= 175.3,b= 175.3,c= 58.7 Å. Two molecules were identified per asymmetric unit.

A Crystallographic Study of Bis[S-benzyl-5-bromo-2-oxoindolin-3-ylidenemethanehydrazonthioate] Disulfide Solvated with Dimethylsulfoxide

2012 ◽  
Vol 9 (2) ◽  
pp. 87
Author(s):  
Mohd Abdul Fatah Abdul Manan ◽  
M. Ibrahim M. Tahir ◽  
Karen A. Crouse ◽  
Fiona N.-F. How ◽  
David J. Watkin
Keyword(s):  
Crystal Structure ◽  
Hydrogen Bonds ◽  
Solvent Molecule ◽  
Site Occupancy ◽  
Unit Cell Parameters ◽  
Intermolecular Hydrogen Bonds ◽  
Triclinic Space Group ◽  
Cell Parameters ◽  
Crystallographic Study ◽  
Thiol Form

The crystal structure of the title compound has been determined. The compound crystallized in the triclinic space group P -1, Z = 2, V = 1839 .42( 18) A3 and unit cell parameters a= 11. 0460( 6) A, b = 13 .3180(7) A, c=13. 7321 (8) A, a = 80.659(3 )0, b = 69 .800(3 )0 and g = 77 .007 (2)0 with one disordered dimethylsulfoxide solvent molecule with the sulfur and oxygen atoms are distributed over two sites; S101/S102 [site occupancy factors: 0.6035/0.3965] and 0130/0131 [site occupancy factor 0.3965/0.6035]. The C22-S2 l and C 19-S20 bond distances of 1. 779(7) A and 1. 788(8) A indicate that both of the molecules are connected by the disulfide bond [S20-S21 2.055(2) A] in its thiol form. The crystal structure reveals that both of the 5-bromoisatin moieties are trans with respect to the [S21-S20 and CI 9-Nl 8] and [S20-S21 and C22-N23] bonds whereas the benzyl group from the dithiocarbazate are in the cis configuration with respect to [S21-S20 and C19-S44] and [S20-S21 and C22-S36] bonds. The crystal structure is further stabilized by intermolecular hydrogen bonds of N9-H35···O16 formed between the two molecules and N28-H281 ···O130, N28-H281 ···O131 and C4 l-H4 l l ···O 131 with the solvent molecule.

Synchrotron powder diffraction characterization of the zeolite-based (p-N,N-dimethylnitroaniline–mordenite) guest–host phase

2008 ◽  
Vol 64 (6) ◽  
pp. 713-724 ◽  
Author(s):  
Florence Porcher ◽  
Elena Borissenko ◽  
Mohamed Souhassou ◽  
Masaki Takata ◽  
Kenichi Kato ◽  
...  
Keyword(s):  
Powder Diffraction ◽  
Dipole Moments ◽  
Membered Ring ◽  
Unit Cell Parameters ◽  
Cell Parameters ◽  
Crystallographic Study ◽  
Synchrotron Powder Diffraction ◽  
Ring Channel ◽  
New Phase

The crystal structure of a new phase consisting of the inclusion of the hyperpolarizable molecule p-N,N-dimethylnitroaniline (dimethyl-para-nitroaniline or dmpNA) in the large-pore zeolite mordenite (MOR) has been determined from high-resolution synchrotron powder diffraction at 300 and 90 K. The unit-cell parameters and space group at 300 K are similar to those of as-synthesized mordenite. The crystallographic study indicates that the MOR straight channels are almost fully loaded with molecules that are disordered over eight symmetry-related sites. As expected, the molecules are located in the large 12-membered ring channel, at the intersection with the secondary eight-membered channel with which they might form hydrogen bonds. The elongation axes (and then the dipole moments) of the molecules are slightly tilted (28.57°) from [001]. The configuration found suggests an interaction of dmpNA with framework O atoms through its methyl groups.

scholarly journals Crystallization of two operator complexes from theVibrio choleraeHigBA2 toxin–antitoxin module

2015 ◽  
Vol 71 (2) ◽  
pp. 226-233 ◽  
Author(s):  
San Hadži ◽  
Abel Garcia-Pino ◽  
Kenn Gerdes ◽  
Jurij Lah ◽  
Remy Loris
Keyword(s):  
Vibrio Cholerae ◽  
Crystal Form ◽  
Unit Cell ◽  
Dna Duplexes ◽  
Dna Duplex ◽  
Unit Cell Parameters ◽  
Crystal Forms ◽  
Space Group ◽  
Cell Parameters ◽  
Complex Crystals

The HigA2 antitoxin and the HigBA2 toxin–antitoxin complex fromVibrio choleraewere crystallized in complex with their operator box. Screening of 22 different DNA duplexes led to two crystal forms of HigA2 complexes and one crystal form of a HigBA2 complex. Crystals of HigA2 in complex with a 17 bp DNA duplex belong to space groupP3221, with unit-cell parametersa=b= 94.0,c= 123.7 Å, and diffract to 2.3 Å resolution. The second form corresponding to HigA2 in complex with a 19 bp duplex belong to space groupP43212 and only diffract to 3.45 Å resolution. Crystals of the HigBA2 toxin–antitoxin were obtained in complex with a 31 bp duplex and belonged to space groupP41212, with unit-cell parametersa=b= 113.6,c= 121.1 Å. They diffract to 3.3 Å resolution.

scholarly journals Expression, purification, crystallization and crystallographic study of theAspergillus terreusaromatic prenyltransferase AtaPT

2015 ◽  
Vol 71 (7) ◽  
pp. 889-894 ◽  
Author(s):  
Bingquan Gao ◽  
Ridao Chen ◽  
Xiao Liu ◽  
Jungui Dai ◽  
Fei Sun
Keyword(s):  
Aromatic Compounds ◽  
Aspergillus Terreus ◽  
Biological Properties ◽  
Chemical Diversity ◽  
The Self ◽  
Asymmetric Unit ◽  
Unit Cell Parameters ◽  
Cell Parameters ◽  
Crystallographic Study ◽  
Rotation Function

Prenylated aromatics are produced by aromatic prenyltransferases during the secondary metabolism of bacteria, fungi and plants. The prenylation of nonprenylated precursors can lead to great chemical diversity and extensive biological properties.Aspergillus terreusaromatic prenyltransferase (AtaPT), which has recently been discovered and characterized, is such an enzyme and is responsible for the prenylation of various aromatic compounds. Here, recombinant AtaPT was overexpressed inEscherichia coli, purified and crystallized. Diffraction data were collected to a resolution of 1.71 Å and the crystal belonged to space groupP21212, with unit-cell parametersa= 96.2,b = 135.8,c= 69.5 Å, α = β = γ = 90°. Analysis of the calculated Matthews coefficient and the self-rotation function suggested that there are two AtaPT molecules in the asymmetric unit.

scholarly journals Neutron crystallographic study of heterotrimeric glutamine amidotransferase CAB

2019 ◽  
Vol 75 (3) ◽  
pp. 193-196
Author(s):  
Long Li ◽  
Motoyasu Adachi ◽  
Jian Yu ◽  
Koji Kato ◽  
Akira Shinoda ◽  
...  
Keyword(s):  
Neutron Diffraction ◽  
Diffraction Data ◽  
Active Sites ◽  
Neutron Diffraction Data ◽  
Asymmetric Unit ◽  
Unit Cell Parameters ◽  
X Ray ◽  
Cell Parameters ◽  
Crystallographic Study ◽  
Glutamine Amidotransferase

Heterotrimeric glutamine amidotransferase CAB (GatCAB) possesses an ammonia-self-sufficient mechanism in which ammonia is produced and used in the inner complex by GatA and GatB, respectively. The X-ray structure of GatCAB revealed that the two identified active sites of GatA and GatB are markedly distant, but are connected in the complex by a channel of 30 Å in length. In order to clarify whether ammonia is transferred through this channel in GatCAB by visualizing ammonia, neutron diffraction studies are indispensable. Here, GatCAB crystals were grown to approximate dimensions of 2.8 × 0.8 × 0.8 mm (a volume of 1.8 mm3) with the aid of a polymer using microseeding and macroseeding processes. Monochromatic neutron diffraction data were collected using the neutron single-crystal diffractometer BIODIFF at the Heinz Maier-Leibnitz Zentrum, Germany. The GatCAB crystals belonged to space group P212121, with unit-cell parameters a = 74.6, b = 94.5, c = 182.5 Å and with one GatCAB complex (molecular mass 119 kDa) in the asymmetric unit. This study represented a challenge in current neutron diffraction technology.

scholarly journals The Escherichia coli RnlA–RnlB toxin–antitoxin complex: production, characterization and crystallization

2020 ◽  
Vol 76 (1) ◽  
pp. 31-39
Author(s):  
Gabriela Garcia-Rodriguez ◽  
Ariel Talavera Perez ◽  
Albert Konijnenberg ◽  
Frank Sobott ◽  
Jan Michiels ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Bacteriophage T4 ◽  
Native Mass Spectrometry ◽  
Affinity Tag ◽  
Unit Cell Parameters ◽  
Cell Parameters ◽  
His Tag ◽  
Complex Crystals ◽  
Protection Against Infection ◽  
Homogeneous Preparation

The Escherichia coli rnlAB operon encodes a toxin–antitoxin module that is involved in protection against infection by bacteriophage T4. The full-length RnlA–RnlB toxin–antitoxin complex as well as the toxin RnlA were purified to homogeneity and crystallized. When the affinity tag is placed on RnlA, RnlB is largely lost during purification and the resulting crystals exclusively comprise RnlA. A homogeneous preparation of RnlA–RnlB containing stoichiometric amounts of both proteins could only be obtained using a His tag placed C-terminal to RnlB. Native mass spectrometry and SAXS indicate a 1:1 stoichiometry for this RnlA–RnlB complex. Crystals of the RnlA–RnlB complex belonged to space group C2, with unit-cell parameters a = 243.32, b = 133.58, c = 55.64 Å, β = 95.11°, and diffracted to 2.6 Å resolution. The presence of both proteins in the crystals was confirmed and the asymmetric unit is likely to contain a heterotetramer with RnlA2:RnlB2 stoichiometry.

scholarly journals Crystallographic study of a novel DNA-binding domain of human HLTF involved in the template-switching pathway to avoid the replication arrest caused by DNA damage

2015 ◽  
Vol 71 (6) ◽  
pp. 668-670 ◽  
Author(s):  
Yuzu Ikegaya ◽  
Kodai Hara ◽  
Asami Hishiki ◽  
Hideshi Yokoyama ◽  
Hiroshi Hashimoto
Keyword(s):  
Dna Damage ◽  
Dna Binding ◽  
Binding Domain ◽  
Template Switching ◽  
Dna Binding Domain ◽  
Unit Cell Parameters ◽  
Cell Parameters ◽  
Replication Arrest ◽  
Crystallographic Study ◽  
Detailed Function

HLTF is a pivotal protein in the template-switching pathway that allows DNA synthesis to continue even in the presence of DNA damage by utilizing a newly synthesized undamaged strand as a template. HLTF has a novel DNA-binding domain termed HIRAN that has been recently found in various proteins, although its detailed function remains unclear. In this study, the HIRAN domain of human HLTF was successfully crystallized. The crystals belonged to space groupP41212 orP43212, with unit-cell parametersa=b= 130.0,c= 150.1 Å.

A Crystallographic Study of Bis[S-benzyl-5-bromo-2-oxoindolin-3-ylidenemethanehydrazonthioate] DisuIfide Solvated with Dimethylsulfoxide

2012 ◽  
Vol 9 (2) ◽  
pp. 87
Author(s):  
Mohd Abdul Fatah Abdul Manan ◽  
Mohamed Ibrahim Mohamed Tahir ◽  
Karen Anne Crouse ◽  
Fiona Ni Foong How ◽  
David J Watkin
Keyword(s):  
Crystal Structure ◽  
Hydrogen Bonds ◽  
Solvent Molecule ◽  
Site Occupancy ◽  
Unit Cell Parameters ◽  
Intermolecular Hydrogen Bonds ◽  
Triclinic Space Group ◽  
Cell Parameters ◽  
Crystallographic Study ◽  
Thiol Form

The crystal structure of the title compound has been determined. The compound crystallized in the triclinic space group P -1 , Z = 2, V = 1839.42(18) A3 and unit cell parameters a= 11.0460(6) A, b = 13.3180(7) A, c = 13.7321(8) A, a= 80.659(3)° , b= 69.800(3)° and g= 77.007(2)° with one disordered dimethylsulfoxide solvent molecule with the sulfur and oxygen atoms are distributed over two sites; S101/S102 [site occupancy factors: 0.6035/0.3965] and O130/O131 [site occupancy factor 0.3965/0.6035]. The C22-S21 and C19-S20 bond distances of1.779(7) A and 1.788(8) A indicate that both of the molecules are connected by the disulfide bond [S20-S21 2.055(2) A] in its thiol form. The crystal structure reveals that both of the 5-bromoisatin moieties are trans with respect to the [S21-S20 and C19-N18] and [S20-S21 and C22-N23] bonds whereas the benzyl group from the dithiocarbazate are in the cis configuration with respect to [S21-S20 and C19-S44] and [S20-S21 and C22-S36] bonds. The crystal structure is further stabilized by intermolecular hydrogen bonds of N9-H35...O16 formed between the two molecules and N28-H281...O130, N28-H281...O131 and C41-H411...O131 with the solvent molecule.

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