Crystallization and preliminary X-ray studies of β-1,4-galactanase from Aspergillus aculeatus

1999 ◽  
Vol 55 (4) ◽  
pp. 929-930 ◽  
Author(s):  
C. Ryttersgaard ◽  
J.-C. N. Poulsen ◽  
S. Christgau ◽  
T. Sandal ◽  
H. Dalbøge ◽  
...  
Keyword(s):  
Asymmetric Unit ◽  
X Ray Diffraction ◽  
Aspergillus Aculeatus ◽  
Solvent Content ◽  
X Ray ◽  
Space Groups ◽  
Peg 400 ◽  
Cell Dimensions ◽  
Vapour Diffusion ◽  
Unit Cell Dimensions

Recombinant β-1,4-galactanase from Aspergillus aculeatus has been crystallized and characterized by X-ray diffraction. Crystals were obtained in hanging drops by vapour-diffusion under the conditions 30% PEG 400, 0.2 M CaCl2 and 0.1 M Na HEPES buffered to pH 7.5. The crystals diffract to 2.3 Å resolution and belong to one of the orthorhombic space groups I222 or I212121. The unit-cell dimensions are a = 60.42, b = 88.94 and c = 129.08 Å. With one molecule in the asymmetric unit, the corresponding solvent content is ∼48%.

Crystallization and preliminary X-ray diffraction of Trypanosoma cruzi dUTPase

1999 ◽  
Vol 55 (2) ◽  
pp. 528-530 ◽  
Author(s):  
V. Bernier-Villamor ◽  
A. Camacho ◽  
D. González-Pacanowska ◽  
E. Cedergren-Zeppezauer ◽  
A. Antson ◽  
...  
Keyword(s):  
Trypanosoma Cruzi ◽  
Unit Cell ◽  
The Self ◽  
Asymmetric Unit ◽  
X Ray Diffraction ◽  
Solvent Content ◽  
X Ray ◽  
Cell Dimensions ◽  
Unit Cell Dimensions ◽  
Rotation Function

Crystals of Trypanosoma cruzi dUTPase have been grown. Two different morphologies are observed, depending on the molecular weight of the PEG used as precipitating agent in the mother liquor, both having a hexagonal unit cell with similar dimensions. Complete X-ray diffraction data have been collected to low resolution for one of the forms. The space group is P6322, with unit-cell dimensions a = 134.15, c = 147.05 Å. Peaks in the self-rotation function and the solvent content are consistent with two molecules of dUTPase per asymmetric unit.

Crystallization and preliminary X-ray analysis of the Escherichia coli UDP-MurNAc-tripeptide D-alanyl-D-alanine-adding enzyme (MurF)

1999 ◽  
Vol 55 (12) ◽  
pp. 2033-2034 ◽  
Author(s):  
Youwei Yan ◽  
Sanjeev Munshi ◽  
Ying Li ◽  
Kelly Ann D. Pryor ◽  
Frank Marsilio ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Asymmetric Unit ◽  
Hanging Drop ◽  
Data Set ◽  
Solvent Content ◽  
X Ray ◽  
Protein Mass ◽  
Cell Dimensions ◽  
Unit Cell Dimensions ◽  
Crystal Volume

Crystals of the Escherichia coli UDP-MurNAc-tripeptide D-Ala-D-Ala-adding protein (MurF), which catalyzes the formation of the last metabolite of the bacterial cell-wall building block, have been grown in hanging-drop vapor-diffusion trials using PEG 8K as a precipitating agent. The crystals belong to hexagonal space group P61 or P65, with unit-cell dimensions a = b = 74, c = 425 Å. The asymmetric unit contains two molecules, with a crystal volume per protein mass (Vm ) of 3.4 Å3 Da−1 and a solvent content of about 64% by volume. A native data set to 2.8 Å resolution has been obtained from a frozen crystal using a synchrotron X-ray source.

Crystallization and preliminary X-ray analysis of the 6-phospho-α-glucosidase from Bacillus subtilis

1999 ◽  
Vol 55 (6) ◽  
pp. 1212-1214 ◽  
Author(s):  
Annabelle Varrot ◽  
Hiroki Yamamoto ◽  
Junichi Sekiguchi ◽  
John Thompson ◽  
Gideon J. Davies
Keyword(s):  
Bacillus Subtilis ◽  
Single Molecule ◽  
Asymmetric Unit ◽  
X Ray Diffraction ◽  
Hanging Drop ◽  
Phosphotransferase System ◽  
X Ray ◽  
Cell Dimensions ◽  
Hanging Drop Method ◽  
Unit Cell Dimensions

6-Phospho-α-glucosidase (GlvA) is the protein involved in the dissimilation of α-glycosides accumulated via a phosphoenolpyruvate-dependent maltose phosphotransferase system (PEP-PTS) in Bacillus subtilis. The purified enzyme has been crystallized in a form suitable for X-ray diffraction analysis. Thin rod-like crystals have been grown by the hanging-drop method in the presence of manganese and NAD. They diffract beyond 2.2 Å using synchrotron radiation and belong to the space group I222 (or its enantiomorph) with unit-cell dimensions a = 83.26, b = 102.56, c = 145.31 Å and contain a single molecule of GlvA in the asymmetric unit.

Infrared and Raman spectra and X-ray diffraction studies of solid lead(II) carbonates

1983 ◽  
Vol 61 (3) ◽  
pp. 494-502 ◽  
Author(s):  
Murray H. Brooker ◽  
S. Sunder ◽  
Peter Taylor ◽  
Vincent J. Lopata
Keyword(s):  
Unit Cell ◽  
Spectral Features ◽  
Infrared And Raman Spectra ◽  
X Ray Diffraction ◽  
X Ray ◽  
Space Groups ◽  
Carbonate Ions ◽  
Cell Dimensions ◽  
Unit Cell Dimensions ◽  
Sodium And Potassium

Four basic lead carbonates were prepared and identified by X-ray powder diffractometry. These were hydrocerussite (Pb3(OH)2(CO3)2), plumbonacrite (Pb10O(OH)6(CO3)6), and the two adducts MOH•2PbCO3 (M = Na, K). New diffraction data are presented for the latter two compounds; they both have primitive hexagonal lattices with two formula units per unit cell. The unit cell dimensions of the sodium and potassium compounds are a = 5.273 ± 0.002 Å, c = 13.448 ± 0.005 Å and a = 5.348 ± 0.002 Å, c = 13.990 ± 0.005 Å, respectively. Six possible space groups are discussed.Raman and infrared spectra are reported for all four compounds, and compared with those of cerussite (PbCO3); assignment of the spectral features is discussed. Vibrational spectra of the two MOH adducts indicate that they are isostructural, and that the structure contains a well-defined lead sub-lattice, consistent with the X-ray data. The spectra of hydrocerussite and plumbonacrite indicate that lead is present as oxygen-bridged polymeric moieties in these solids. The carbonate ions occupy two and three independent sites in hydrocerussite and plumbonacrite, respectively.

Crystallization and preliminary X-ray diffraction studies of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Methanothermus fervidus

1999 ◽  
Vol 55 (7) ◽  
pp. 1353-1355 ◽  
Author(s):  
C. Charron ◽  
F. Talfournier ◽  
M. N. Isupov ◽  
G. Branlant ◽  
J. A. Littlechild ◽  
...  
Keyword(s):  
Diffusion Method ◽  
Asymmetric Unit ◽  
X Ray Diffraction ◽  
Hanging Drop ◽  
Data Set ◽  
Hyperthermophilic Archaeon ◽  
X Ray ◽  
Cell Dimensions ◽  
Methanothermus Fervidus ◽  
Unit Cell Dimensions

The homotetrameric holo-D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Methanothermus fervidus has been crystallized in the presence of NADP+ using the hanging-drop vapour-diffusion method. Crystals grew from a solution containing 2-methyl-2,4-pentanediol and magnesium acetate. A native data set has been collected to 2.1 Å using synchrotron radiation and cryocooling. Diffraction data have been processed in the orthorhombic system (space group P21212) with unit-cell dimensions a = 136.7, b = 153.3, c = 74.9 Å and one tetramer per asymmetric unit.

Crystallization and preliminary X-ray crystallographic analysis of the unusual ferritin from Listeria innocua

1999 ◽  
Vol 55 (2) ◽  
pp. 552-553 ◽  
Author(s):  
Andrea Ilari ◽  
Carmelinda Savino ◽  
Simonetta Stefanini ◽  
Emilia Chiancone ◽  
Demetrius Tsernoglou
Keyword(s):  
Packing Density ◽  
Crystallographic Analysis ◽  
Listeria Innocua ◽  
Diffusion Method ◽  
Asymmetric Unit ◽  
Orthorhombic Space Group ◽  
X Ray ◽  
Cell Dimensions ◽  
Vapour Diffusion ◽  
Unit Cell Dimensions

Single crystals of ferritin extracted from Listeria innocua have been obtained by the vapour-diffusion method using PEG 1000 as precipitant. The crystals are orthorhombic, space group P212121, with unit-cell dimensions a = 87.7, b = 137.5, c = 173.1 Å. The crystals diffract to 2.9 Å resolution on a rotating-anode X-ray source and to 2.35 Å resolution on a synchrotron X-ray source. The asymmetric unit contains one molecule formed by 12 subunits, corresponding to a packing density of 2.41 Å3 Da−1

Crystallization and preliminary X-ray studies of hORF6, a novel human antioxidant enzyme

1998 ◽  
Vol 54 (3) ◽  
pp. 436-436 ◽  
Author(s):  
Hee-Jeong Choi ◽  
Sang Won Kang ◽  
Chul-Hak Yang ◽  
Sue Goo Rhee ◽  
Seong-Eon Ryu
Keyword(s):  
Antioxidant Enzyme ◽  
Unit Cell ◽  
X Rays ◽  
Asymmetric Unit ◽  
Data Set ◽  
X Ray ◽  
Space Groups ◽  
Cell Dimensions ◽  
Hanging Drop Method ◽  
Unit Cell Dimensions

HORF6 is a member of the novel antioxidant enzyme family found in humans. A recombinant form of hORF6 expressed and purified from E. coli has been crystallized by the hanging-drop method using various PEG's as precipitating agents. HORF6 crystallizes in two different monoclinic space groups, P21 and C2. The P21 crystals have unit-cell dimensions of a = 47.85, b = 75.17, c = 63.30 Å and β = 110.21° and contain two monomers per asymmetric unit, while the C2 crystals have unit-cell dimensions of a = 165.27, b = 95.44, c = 166.44 Å and β = 128.97° and contain more than six monomers per asymmetric unit. The P21 crystals with the smaller unit cell diffract X-rays better and behave well for the X-ray analysis. A native data set from a single crystal of the P21 space group gas been collected to 2.0 Å resolution.

Crystallization and preliminary X-ray diffraction data of the complex of recombinant tick anticoagulant peptide (rTAP) and bovine factor Xa

1999 ◽  
Vol 55 (4) ◽  
pp. 862-864 ◽  
Author(s):  
Anzhi Wei ◽  
Angela Smallwood ◽  
Richard S. Alexander ◽  
Jodie Duke ◽  
Harold Ross ◽  
...  
Keyword(s):  
Polyethylene Glycol ◽  
Factor Xa ◽  
Asymmetric Unit ◽  
X Ray Diffraction ◽  
Crystal Forms ◽  
X Ray ◽  
Cell Dimensions ◽  
Unit Cell Dimensions ◽  
Tick Anticoagulant Peptide ◽  
Bovine Factor

The complex of bovine factor Xa and recombinant tick anticoagulant peptide (rTAP) was crystallized in two different crystal forms using polyethylene glycol as a precipitant. Form I belongs to space group P42212 with unit-cell dimensions a = b = 133.1, c = 68.8 Å. It contains one complex per asymmetric unit and diffracts to 3.0 Å resolution. Form II belongs to P41212 (or P43212) with dimensions a = b = 126.5, c = 146.7 Å; it contains two complexes per asymmetric unit and diffracts to 2.5 Å. The crystals of both forms consist of factor Xa (MW  = 45.3 kDa) and rTAP (MW = 6.7 kDa).

Crystallization and preliminary X-ray analysis of porcine muscle prolyl oligopeptidase

1998 ◽  
Vol 54 (6) ◽  
pp. 1414-1415 ◽  
Author(s):  
Zsolt Böcskei ◽  
Mónika Fuxreiter ◽  
Gábor Náray-Szabó ◽  
Erika Szabó ◽  
László Polgár
Keyword(s):  
Calcium Acetate ◽  
Asymmetric Unit ◽  
X Ray Diffraction ◽  
Single Chain ◽  
Prolyl Oligopeptidase ◽  
Solvent Content ◽  
X Ray ◽  
Cell Dimensions ◽  
Pig Muscle ◽  
Peg 8000

Prolyl oligopeptidase from pig muscle has been crystallized in complex with an inhibitor, using PEG 8000 and calcium acetate as precipitants. The crystals are orthorombic and the space group is P212121 with cell dimensions a = 111.8, b = 101.8, c = 72.4 Å. The asymmetric unit contains a single chain of prolyl oligopeptidase, corresponding to a specific volume of 2.55 Å3 Da−1 and a solvent content of 52%. The observed diffraction pattern extends to 2.3 Å resolution and the native crystals are well suited for structural analysis by X-ray diffraction methods.

Crystallization and preliminary X-ray diffraction studies of human catalase

1999 ◽  
Vol 55 (9) ◽  
pp. 1614-1615 ◽  
Author(s):  
R. A. P. Nagem ◽  
E. A. L. Martins ◽  
V. M. Gonçalves ◽  
R. Aparício ◽  
I. Polikarpov
Keyword(s):  
Search Model ◽  
Molecular Replacement ◽  
X Ray Diffraction ◽  
Beef Liver ◽  
X Ray ◽  
Diffusion Technique ◽  
Cell Dimensions ◽  
Synchrotron Radiation Diffraction ◽  
Replacement Solution ◽  
Unit Cell Dimensions

The enzyme catalase (H2O2–H2O2 oxidoreductase; E.C. 11.1.6) was purified from haemolysate of human placenta and crystallized using the vapour-diffusion technique. Synchrotron-radiation diffraction data have been collected to 1.76 Å resolution. The enzyme crystallized in the space group P212121, with unit-cell dimensions a = 83.6, b = 139.4, c = 227.5 Å. A molecular-replacement solution of the structure has been obtained using beef liver catalase (PDB code 4blc) as a search model.

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