scholarly journals Two crystal forms of a helix-rich fatty acid- and retinol-binding protein, Na-FAR-1, from the parasitic nematodeNecator americanus

2012 ◽  
Vol 68 (7) ◽  
pp. 835-838 ◽  
Author(s):  
Mads Gabrielsen ◽  
M. Florencia Rey-Burusco ◽  
Kate Griffiths ◽  
Andrew J. Roe ◽  
Alan Cooper ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Structural Information ◽  
Binding Protein ◽  
Crystal Form ◽  
Blood Feeding ◽  
Unit Cell ◽  
Retinol Binding Protein ◽  
Unit Cell Parameters ◽  
Space Group ◽  
Cell Parameters

Na-FAR-1 is an unusual α-helix-rich fatty acid- and retinol-binding protein fromNecator americanus, a blood-feeding intestinal parasitic nematode of humans. It belongs to the FAR protein family, which is unique to nematodes; no structural information is available to date for FAR proteins from parasites. Crystals were obtained with two different morphologies that corresponded to different space groups. Crystal form 1 exhibited space groupP432 (unit-cell parametersa = b = c = 120.80 Å, α = β = γ = 90°) and diffracted to 2.5 Å resolution, whereas crystal form 2 exhibited space groupF23 (unit-cell parametersa = b = c = 240.38 Å, α = β = γ = 90°) and diffracted to 3.2 Å resolution. Crystal form 2 showed signs of significant twinning.

Crystallization and preliminary X-ray study of two crystal forms of Klebsiella oxytoca diol dehydratase–cyanocobalamin complex

1999 ◽  
Vol 55 (4) ◽  
pp. 907-909 ◽  
Author(s):  
Jun Masuda ◽  
Tetsuya Yamaguchi ◽  
Takamasa Tobimatsu ◽  
Tetsuo Toraya ◽  
Kyoko Suto ◽  
...  
Keyword(s):  
Klebsiella Oxytoca ◽  
Crystal Form ◽  
Unit Cell ◽  
Unit Cell Parameters ◽  
Crystal Forms ◽  
Space Group ◽  
X Ray ◽  
Cell Parameters ◽  
Diol Dehydratase ◽  
Replacement Method

Two crystal forms of Klebsiella oxytoca diol dehydratase complexed with cyanocobalamin have been obtained and preliminary crystallographic experiments have been performed. The crystals belong to two different space groups, depending on the crystallization conditions. One crystal (form I) belongs to space group P212121 with unit-cell parameters a = 76.2, b = 122.3, c = 209.6 Å, and diffracts to 2.2 Å resolution using an X-ray beam from a synchrotron radiation source. The other crystal (form II) belongs to space group P21 with unit-cell parameters a = 75.4, b = 132.7, c = 298.8 Å, β = 91.9°, and diffracts to 3.0 Å resolution. For the purpose of structure determination, a heavy-atom derivative search was carried out and some mercuric derivatives were found to be promising. Structure analysis by the multiple isomorphous replacement method is now under way.

scholarly journals Crystals of the Arp2/3 complex in two new space groups with structural information about actin-related protein 2 and potential WASP binding sites

2015 ◽  
Vol 71 (9) ◽  
pp. 1161-1168 ◽  
Author(s):  
Christopher T. Jurgenson ◽  
Thomas D. Pollard
Keyword(s):  
Binding Site ◽  
Structural Information ◽  
Unit Cell ◽  
Molecular Structures ◽  
Asymmetric Unit ◽  
Unit Cell Parameters ◽  
Space Group ◽  
Space Groups ◽  
Cell Parameters ◽  
New Space

Co-crystals of the bovine Arp2/3 complex with the CA motif from N-WASP in two new space groups were analyzed by X-ray diffraction. The crystals in the orthorhombic space groupP212121contained one complex per asymmetric unit, with unit-cell parametersa= 105.48,b= 156.71,c= 177.84 Å, and diffracted to 3.9 Å resolution. The crystals in the tetragonal space groupP41contained two complexes per asymmetric unit, with unit-cell parametersa=b= 149.93,c = 265.91 Å, and diffracted to 5.0 Å resolution. The electron-density maps of both new crystal forms had densities for small segments of subdomains 1 and 2 of Arp2. Both maps had density at the binding site on Arp3 for the C-terminal EWE tripeptide from N-WASP and a binding site proposed for the C motif of N-WASP in the barbed-end groove of Arp2. The map from the tetragonal crystal form had density near the barbed end of Arp3 that may correspond to the C helix of N-WASP. The noise levels and the low resolution of the maps made the assignment of specific molecular structures for any of these CA peptides impossible.

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 and crystallization of the phosphate-binding PstS protein fromPseudomonas aeruginosa

2014 ◽  
Vol 70 (7) ◽  
pp. 906-910 ◽  
Author(s):  
Avi Neznansky ◽  
Yarden Opatowsky
Keyword(s):  
Crystal Form ◽  
Phosphate Transport ◽  
Unit Cell ◽  
Asymmetric Unit ◽  
Unit Cell Parameters ◽  
Orthorhombic Space Group ◽  
Solvent Content ◽  
Space Group ◽  
Cell Parameters ◽  
Crystal Volume

Pseudomonas aeruginosa(PA) infections pose a serious threat to human health. PA is a leading cause of fatal lung infections in cystic fibrosis and immune-suppressed patients, of sepsis in burn victims and of nosocomial infections. An important element in PA virulence is its ability to establish biofilms that evade suppression by the host's immune system and antibiotics. PstS, a periplasmic subunit of the Pst phosphate-transport system of PA, plays a critical role in the establishment of biofilms. In some drug-resistant PA strains, PstS is secreted in large quantities from the bacteria, where it participates in the assembly of adhesion fibres that enhance bacterial virulence. In order to understand the dual function of PstS in biofilm formation and phosphate transport, the crystal structure of PA PstS was determined. Here, the overexpression inEscherichia coliand purification of PA PstS in the presence of phosphate are described. Two crystal forms were obtained using the vapour-diffusion method at 20°C and X-ray diffraction data were collected. The first crystal form belonged to the centred orthorhombic space groupC2221, with unit-cell parametersa= 67.5,b= 151.3,c= 108.9 Å. Assuming the presence of a dimer in the asymmetric unit gives a crystal volume per protein weight (VM) of 2.09 Å3 Da−1and a solvent content of 41%. The second crystal form belonged to the primitive orthorhombic space groupP212121, with unit-cell parametersa= 35.4,b= 148.3,c= 216.7 Å. Assuming the presence of a tetramer in the asymmetric unit gives a crystal volume per protein weight (VM) of 2.14 Å3 Da−1and a solvent content of 42.65%. A pseudo-translational symmetry is present in theP212121crystal form which is consistent with a filamentous arrangement of PstS in the crystal lattice.

scholarly journals Crystallization and preliminary X-ray diffraction analysis ofHypocrea jecorinaCel7A in two new crystal forms

2014 ◽  
Vol 70 (6) ◽  
pp. 773-776 ◽  
Author(s):  
Annette M. Bodenheimer ◽  
Matthew J. Cuneo ◽  
Paul D. Swartz ◽  
Junhong He ◽  
Hugh M. O'Neill ◽  
...  
Keyword(s):  
Catalytic Domain ◽  
Crystal Form ◽  
Unit Cell ◽  
Carbohydrate Binding ◽  
X Rays ◽  
Cellobiohydrolase I ◽  
Unit Cell Parameters ◽  
Crystal Forms ◽  
Space Group ◽  
Cell Parameters

Cel7A (previously known as cellobiohydrolase I) fromHypocrea jecorinawas crystallized in two crystalline forms, neither of which have been previously reported. Both forms co-crystallize under the same crystallization conditions. The first crystal form belonged to space groupC2, with unit-cell parametersa= 152.5,b= 44.9,c= 57.6 Å, β = 101.2°, and diffracted X-rays to 1.5 Å resolution. The second crystal form belonged to space groupP6322, with unit-cell parametersa=b≃ 155,c≃ 138 Å, and diffracted X-rays to 2.5 Å resolution. The crystals were obtained using full-length Cel7A, which consists of a large 434-residue N-terminal catalytic domain capable of cleaving cellulose, a 27-residue flexible linker and a small 36-residue C-terminal carbohydrate-binding module (CBM). However, a preliminary analysis of the electron-density maps suggests that the linker and CBM are disordered in both crystal forms. Complete refinement and structure analysis are currently in progress.

scholarly journals Crystallization and preliminary X-ray diffraction studies of a novel bacterial esterase

1999 ◽  
Vol 55 (4) ◽  
pp. 915-917 ◽  
Author(s):  
Philip C. Bourne ◽  
Michail N. Isupov ◽  
Jennifer A. Littlechild
Keyword(s):  
Vapour Phase ◽  
Crystal Form ◽  
Unit Cell ◽  
X Ray Diffraction ◽  
Unit Cell Parameters ◽  
Data Set ◽  
Space Group ◽  
X Ray ◽  
Cell Parameters ◽  
Phase Calculation

A novel bacterial esterase has been crystallized in two forms suitable for X-ray diffraction studies. Crystals have been obtained by vapour-phase diffusion at 290 K using ammonium sulfate as precipitant. The first crystals grew in space group C2 with unit-cell parameters a = 134.7, b = 55.8, c = 110.3 Å, β = 125.1°. A monoclinic data set has been collected to 2.0 Å resolution. Microseeding yielded a second crystal form which grew in space group P212121 with unit-cell parameters a = 57.1, b = 115.4, c = 130.4 Å. Native data from these crystals have been collected to 1.6 Å resolution. A molecular envelope has been determined using an uranyl acetate derivative for phase calculation.

scholarly journals Crystal structure of barley agmatine coumaroyltransferase, an N-acyltransferase from the BAHD superfamily

2020 ◽  
Vol 76 (12) ◽  
pp. 590-596
Author(s):  
Miyo Yamane ◽  
Mihoko Takenoya ◽  
Shunsuke Yajima ◽  
Masayuki Sue
Keyword(s):  
Crystal Structure ◽  
Hordeum Vulgare ◽  
Secondary Metabolites ◽  
Secondary Metabolism ◽  
Structural Information ◽  
Unit Cell ◽  
Monoclinic Space Group ◽  
Unit Cell Parameters ◽  
Space Group ◽  
Cell Parameters

The enzymes of the BAHD superfamily, a large group of acyl-CoA-dependent acyltransferases in plants, are involved in the biosynthesis of diverse secondary metabolites. While the structures of several O-acyltransferases from the BAHD superfamily, such as hydroxycinnamoyl-CoA shikimate hydroxycinnamoyl transferase, have been elucidated, no structural information on N-acyltransferases is available. Hordeum vulgare agmatine coumaroyltransferase (HvACT) is an N-acyltransferase from the BAHD superfamily and is one of the most important enzymes in the secondary metabolism of barley. Here, an apo-form structure of HvACT is reported as the first structure of an N-acyltransferase from the BAHD superfamily. HvACT crystals diffracted to 1.8 Å resolution and belonged to the monoclinic space group P21, with unit-cell parameters a = 57.6, b = 59.5, c = 73.6 Å, α = 90, β = 91.3 , γ = 90°. Like other known BAHD superfamily structures, HvACT contains two domains that adopt a two-layer αβ-sandwich architecture and a solvent-exposed channel that penetrates the enzyme core.

Structure of buffalo lactoferrin at 2.5 Å resolution using crystals grown at 303 K shows different orientations of the N and C lobes

1999 ◽  
Vol 55 (11) ◽  
pp. 1805-1813 ◽  
Author(s):  
Subramanian Karthikeyan ◽  
Murugan Paramasivam ◽  
Savita Yadav ◽  
Alagiri Srinivasan ◽  
Tej P. Singh
Keyword(s):  
Crystal Structures ◽  
Crystal Form ◽  
Unit Cell ◽  
The Other ◽  
Unit Cell Parameters ◽  
Orthorhombic Space Group ◽  
Space Group ◽  
Cell Parameters ◽  
Other Hand ◽  
External Conditions

The structure of buffalo lactoferrin has been determined at 303 K. The crystals belong to orthorhombic space group P212121, with unit-cell parameters a = 77.5, b = 91.0, c = 131.5 Å and Z = 4. The structure has been refined to an R factor of 0.187. The overall structure of the protein is similar to its structure determined at 277 K in a different crystal form. However, the lobe orientations in the two structures differ by 9.0°, suggesting significant inter-lobe flexibility in this family of proteins. The inter-lobe interactions are predominantly hydrophobic and could act as a cushion for a change in orientation under the influence of external conditions. On the other hand, the domain arrangements are found to be similar in 277 and 303 K crystal structures, with orientations differing by 1.5 and 1.0° in the N and C lobes, respectively. The results of these investigations suggest that the increase in temperature helps in the production of better quality crystals.

scholarly journals New crystal structures of adenylate kinase fromStreptococcus pneumoniaeD39 in two conformations

2014 ◽  
Vol 70 (11) ◽  
pp. 1468-1471
Author(s):  
Trung Thanh Thach ◽  
Sangho Lee
Keyword(s):  
Crystal Structures ◽  
Adenylate Kinase ◽  
Bound States ◽  
Critical Role ◽  
Unit Cell ◽  
Unit Cell Parameters ◽  
Space Group ◽  
Cell Parameters ◽  
Ligand Free ◽  
Adenylate Kinases

Adenylate kinases (AdKs; EC 2.7.3.4) play a critical role in intercellular homeostasis by the interconversion of ATP and AMP to two ADP molecules. Crystal structures of adenylate kinase fromStreptococcus pneumoniaeD39 (SpAdK) have recently been determined using ligand-free and inhibitor-bound crystals belonging to space groupsP21andP1, respectively. Here, new crystal structures of SpAdK in ligand-free and inhibitor-bound states determined at 1.96 and 1.65 Å resolution, respectively, are reported. The new ligand-free crystal belonged to space groupC2, with unit-cell parametersa= 73.5,b= 54.3,c= 62.7 Å, β = 118.8°. The new ligand-free structure revealed an open conformation that differed from the previously determined conformation, with an r.m.s.d on Cαatoms of 1.4 Å. The new crystal of the complex with the two-substrate-mimicking inhibitorP1,P5-bis(adenosine-5′-)pentaphosphate (Ap5A) belonged to space groupP1, with unit-cell parametersa= 53.9,b= 62.3,c= 63.0 Å, α = 101.9, β = 112.6, γ = 89.9°. Despite belonging to the same space group as the previously reported crystal, the new Ap5A-bound crystal contains four molecules in the asymmetric unit, compared with two in the previous crystal, and shows slightly different lattice contacts. These results demonstrate that SpAdK can crystallize promiscuously in different forms and that the open structure is flexible in conformation.

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