Crystallization and preliminary X-ray diffraction analysis of malic enzyme from pigeon liver

1999 ◽  
Vol 55 (11) ◽  
pp. 1930-1932 ◽  
Author(s):  
Li-Chu Tsai ◽  
Chen-Chin Kuo ◽  
Wei-Yuan Chou ◽  
Gu-Gang Chang ◽  
Hanna S. Yuan
Keyword(s):  
Malic Enzyme ◽  
Diffusion Method ◽  
X Ray Diffraction ◽  
Hanging Drop ◽  
Crystal Forms ◽  
X Ray ◽  
Cell Dimensions ◽  
Unit Cells ◽  
Unit Cell Dimensions ◽  
Pigeon Liver

Recombinant pigeon-liver malic enzyme was expressed in Escherichia coli and purified to homogeneity. Two different crystal forms were grown by the hanging-drop vapour-diffusion method. Both types of crystals belong to the tetragonal space group P4222, with unit-cell dimensions a = b = 163.8, c = 174.3 Å for the octahedral crystals and a = b = 124.5, c = 179.2 Å for the rod-like crystals. X-ray diffraction data were collected at 100 K using a synchrotron-radiation X-ray source. The Matthews parameter suggests that there are four and two molecules per asymmetric unit for the larger and the smaller tetragonal unit cells, 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 studies of the basic lectin from the seeds of Artocarpus hirsuta

1999 ◽  
Vol 55 (6) ◽  
pp. 1204-1205 ◽  
Author(s):  
K. N. Rao ◽  
Madhura M. Gurjar ◽  
Sushama M. Gaikwad ◽  
M. Islam Khan ◽  
C. G. Suresh
Keyword(s):  
Unit Cell ◽  
Diffusion Method ◽  
Hanging Drop ◽  
Crystal Forms ◽  
Space Group ◽  
X Ray ◽  
Hexagonal Form ◽  
Cell Dimensions ◽  
Crystallization Conditions ◽  
Unit Cell Dimensions

The basic lectin from Artocarpus hirsuta specific towards methyl α-galactose has been purified and crystallized using the hanging-drop vapour-diffusion method with ammonium sulfate as precipitant. Three different crystal forms, orthorhombic I, orthorhombic II and hexagonal, were grown under the same crystallization conditions. The orthorhombic forms belonged to space group P212121 with unit-cell dimensions a = 92.9, b = 99.8, c = 166.2 Å and a = 89.9, b = 121.9, c = 131.6 Å, respectively. The unit-cell dimensions of the hexagonal form were a = b = 84.1 and c = 271.7 Å and the space group was P6122.

Crystallization and preliminary X-ray diffraction studies of cytochrome c 6 from Porphyra yezoensis

2000 ◽  
Vol 56 (1) ◽  
pp. 79-80
Author(s):  
Tomokazu Sasaki ◽  
Megumi Nakahara ◽  
Aya Matsuda ◽  
Takenobu Yamasaki ◽  
Sakae Katoh ◽  
...  
Keyword(s):  
Porphyra Yezoensis ◽  
Unit Cell ◽  
Diffusion Method ◽  
X Ray Diffraction ◽  
Crystal Forms ◽  
Space Group ◽  
Cell Dimensions ◽  
Tetragonal Crystals ◽  
Tetragonal Form ◽  
Unit Cell Dimensions

Cytochrome c 6 from the red alga Porphyra yezoensis has been purified and crystallized by the sitting-drop vapour-diffusion method. Two different crystal forms, tetragonal and orthorhombic, were obtained. The tetragonal crystals belong to space group P41212 or P43212, with unit-cell dimensions a = 49.33 (2), c = 83.70 (10) Å. The orthorhombic crystals belong to space group P212121, with unit-cell dimensions a = 46.74 (2), b = 49.42 (1), c = 37.11 (1) Å. Absorption spectra of the crystals showed that the tetragonal form was oxidized and the orthorhombic form was reduced.

Crystallization and preliminary X-ray diffraction studies of C4-form phosphoenolpyruvate carboxylase from maize

1999 ◽  
Vol 55 (11) ◽  
pp. 1937-1938 ◽  
Author(s):  
Hiroyoshi Matsumura ◽  
Takahiro Nagata ◽  
Mika Terada ◽  
Shunsuke Shirakata ◽  
Tsuyoshi Inoue ◽  
...  
Keyword(s):  
Acid Metabolism ◽  
Diffusion Method ◽  
X Ray Diffraction ◽  
Cam Plants ◽  
X Ray ◽  
Cell Dimensions ◽  
Maize Leaves ◽  
Key Enzyme ◽  
Unit Cell Dimensions ◽  
Peg 8000

Phosphoenolpyruvate carboxylase is a key enzyme in the fixation of atmospheric CO2 in C4 and crassulacean acid metabolism (CAM) plants. The enzyme catalyzes the irreversible carboxylation of phosphoenolpyruvate to form oxaloacetate and inorganic phosphate, the first committed step in the fixation of external CO2 in these plants. The enzyme has been isolated from maize leaves and crystallized using the hanging-drop vapour-diffusion method with PEG 8000 as a precipitant at pH 7.5. The crystals belong to space group C2221, with unit-cell dimensions a = 160.2, b = 175.6, c = 255.5 Å, and diffract to 3.2 Å resolution.

Structural study in the oligomethylene dithiobenzoate series, nDBS, where n, the number of methylene groups, is odd

1992 ◽  
Vol 70 (3) ◽  
pp. 900-909 ◽  
Author(s):  
Claude Leblanc ◽  
François Brisse
Keyword(s):  
Crystal Structure ◽  
X Ray Diffraction ◽  
Aromatic Rings ◽  
Monoclinic System ◽  
X Ray ◽  
Cell Dimensions ◽  
Unit Cells ◽  
Methylene Groups ◽  
Unit Cell Dimensions ◽  
Centrosymmetric Dimers

Model compounds of the poly(oligomethylene thioterephthalates) have been synthesized and characterized by X-ray diffraction analyses. The pink n-methylenedithiobenzoates, obtained for n = 3, 5, 7, and 9, all have a low melting point of about 320–330 K. They all crystallize in the monoclinic system, space group P21/c. The a and b unit cell dimensions vary little while the c dimension increases monotonically as n changes from 3 to 9. The crystal structure of the four compounds were established from low-temperature X-ray intensities. Except for the lengthening of the methylenic sequence, the four molecules studied here are isostructural. One of the thiobenzoate groups of the molecules is coplanar with all the methylenic carbons, while the other thiobenzoate group is at 90° from the above plane of atoms. The methylenic sequence has the same conformation. It may be described by g+(t)n, where n is the number of methylene groups. Thus, the four compounds belong to a crystallographically homologous series. The molecules form centrosymmetric "dimers," which, in turn, are herring-bone packed in their respective unit cells. In each "dimmer" two aromatic rings are across from one another while being mutually perpendicular. On the basis of the above results, one proposes three potentially acceptable structures for the parent poly(oligomethylene thioterephthalates). Keywords: dithiobenzoate, methylene sequence, crystal structure, poly(oligomethylene thioterephthalate).

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.

Initiating a crystallographic study of UDP-galactopyranose mutase from Escherichia coli

1999 ◽  
Vol 55 (2) ◽  
pp. 399-402 ◽  
Author(s):  
Stephen A. McMahon ◽  
Gordon A. Leonard ◽  
Louise V. Buchanan ◽  
Marie-France Giraud ◽  
James H. Naismith
Keyword(s):  
Thin Plates ◽  
Diffusion Method ◽  
Data Sets ◽  
X Ray Diffraction ◽  
Orthorhombic Space Group ◽  
X Ray ◽  
Crystallographic Study ◽  
Cell Dimensions ◽  
Unit Cell Dimensions ◽  
Platinum Derivative

UDP-galactopyranose mutase, the enzyme responsible for the conversion of UDP-galactopyranose to UDP-galactofuranose, has been crystallized in a form suitable for X-ray diffraction studies. UDP-galactofuranose is a key component of mycobacterial cell walls. Crystals of both the native protein and a selenomethionine variant have been grown by the vapour-diffusion method in hanging drops, and diffract to beyond 3.0 Å using synchrotron radiation. Equilibration was against a solution of 20%(w/v) polyethylene glycol (4K), 12%(v/v) 2-propanol, 0.1 M HEPES pH 7.6 at 293.5 K. Crystals grow as thin plates of dimensions 0.4 × 0.2 × ∼0.02 mm. They are orthorhombic, space group P21, with unit-cell dimensions a = 71.12, b = 58.42, c = 96.38 Å, β = 96.38°. 92% (native) and 94% (selenomethionine) complete data sets have been recorded to 2.9 Å (R merge = 5.0%) and 3.0 Å (R merge = 6.9%), respectively. The Matthews coefficient is 2.35 Å3 Da−1 for a dimer in the asymmetric unit, the solvent content being 47%. Diffraction data have also been recorded on a putative platinum derivative to 3.5 Å.

Purification, crystallization and preliminary X-ray crystallographic analysis of recombinant murine Golgi mannosidase IA, a class I α-mannosidase involved in Asn-linked oligosaccharide maturation

1999 ◽  
Vol 55 (2) ◽  
pp. 571-573 ◽  
Author(s):  
Francois Vallée ◽  
Anita Lal ◽  
Kelley W. Moremen ◽  
P. Lynne Howell
Keyword(s):  
Transmembrane Domain ◽  
Crystallographic Analysis ◽  
Class I ◽  
Diffusion Method ◽  
Type Ii ◽  
Asymmetric Unit ◽  
Hanging Drop ◽  
X Ray ◽  
Cell Dimensions ◽  
Unit Cell Dimensions

Golgi mannosidase IA is a class I α-mannosidase which catalyzes the conversion of Man9GlcNAc2 or Man8GlcNAc2 oligosaccharide substrates to Man5GlcNAc2 during the maturation of Asn-linked oligosaccharides. The enzyme is a type II membrane protein, and a recombinant form of mannosidase IA from mouse, lacking the transmembrane domain, has been expressed in Pichia pastoris, purified to homogeneity and crystallized by the hanging-drop vapor-diffusion method. The crystals grow as thin rods, with unit-cell dimensions a = 54.9, b = 135.01, c = 69.9 Å. The crystals exhibit the symmetry of space group P2221 and diffract to 2.8 Å resolution. The asymmetric unit contains one monomer (∼53 kDa) and has a solvent content of 59%.

Crystallization and preliminary X-ray analysis of thiaminase I from Bacillus thiaminolyticus: space group change upon freezing of crystals

1998 ◽  
Vol 54 (3) ◽  
pp. 448-450 ◽  
Author(s):  
Nino Campobasso ◽  
Jakob Begun ◽  
Colleen A. Costello ◽  
Tadhg P. Begley ◽  
Steven E. Ealick
Keyword(s):  
Sodium Acetate ◽  
Crystal Form ◽  
Unit Cell ◽  
Diffusion Method ◽  
Crystal Forms ◽  
Space Group ◽  
X Ray ◽  
Cell Dimensions ◽  
Thiaminase I ◽  
Unit Cell Dimensions

Thiaminase I (Mr = 42 100) from B. thiaminolyticus, expressed in E. coli, has been crystallized by the vapor-diffusion method. Three crystal forms, two of which grew from 0.1 M sodium acetate (pH = 4.6), 0.2 M ammonium sulfate and 30%(w/v) PEG 2000, have been examined by X-ray analysis. One crystal form diffracted to 2.5 Å at room temperature, was orthorhombic, and had unit-cell edges of a = 87.7, b = 120.5 and c = 76.7 Å with space group P212121. A self-Patterson map showed a strong peak indicating noncrystallographic translational pseudosymmetry with (u, v, w) = (0.03, 0.0, 0.5). When these crystals were frozen at liquid-nitrogen temperatures, a second crystal form was observed which had unit-cell dimensions a = 85.5, b = 117.5 and c = 36.6 Å with space group P21212. A third crystal form grew from 0.1 M Tris (pH = 8.5), 0.2 M sodium acetate trihydrate and 28%(w/v) PEG 6000 to produce orthorhombic crystals of space group P212121 with cell edges of a = 114.4, b = 123.1 and c = 92.5 Å.

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).

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