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.

scholarly journals X-ray Crystallographic Study of Ranaconitine

2011 ◽  
Vol 6 (11) ◽  
pp. 1934578X1100601
Author(s):  
Yang Li ◽  
Jun-Hui Zhou ◽  
Gui-Jun Han ◽  
Min-Juan Wang ◽  
Wen-Ji Sun ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Hydrogen Bonds ◽  
Diffraction Analysis ◽  
Critical Role ◽  
X Ray Diffraction ◽  
Monoclinic System ◽  
X Ray ◽  
Crystallographic Study ◽  
Cell Dimensions ◽  
Unit Cell Dimensions

The crystal structure of natural diterpenoid alkaloid ranaconitine isolated from Aconitum sinomontanum Nakai has been determined by single crystal X-ray diffraction analysis. The crystal presents a monoclinic system, space group C2 with Z = 4, unit cell dimensions a = 30.972(19) Å, b = 7.688(5) Å, and c = 19.632(12) Å. Moreover, the intermolecular O–H···O hydrogen bonds and weak π-π interactions play a critical role in expanding the dimensionality.

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.

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.

scholarly journals Pressure-induced polymorphism in cyclopropylamine

2005 ◽  
Vol 61 (6) ◽  
pp. 717-723 ◽  
Author(s):  
Patricia Lozano-Casal ◽  
David R. Allan ◽  
Simon Parsons
Keyword(s):  
Crystal Structure ◽  
Crystal Packing ◽  
Hirshfeld Surface ◽  
Amino Group ◽  
X Ray Diffraction ◽  
Orthorhombic Space Group ◽  
X Ray ◽  
Cell Dimensions ◽  
Graph Set ◽  
Unit Cell Dimensions

The crystal structure of cyclopropylamine at 1.2 GPa has been determined by X-ray diffraction methods. The structure of this phase is orthorhombic, space group Pbca and the unit-cell dimensions are a =  5.0741 (10), b  =  9.7594 (10) and c  =  13.305 (2) Å. Only one of the two H atoms of the amino group actively participates in the formation of the hydrogen-bonded chains, C(2) in graph-set notation, which lie parallel to the crystallographic a axis. Additionally, the topology of the crystal packing is studied using both Voronoi–Dirichlet polyhedra and Hirshfeld surface analyses for the low-temperature and the high-pressure structures of cyclopropylamine and the results are compared.

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 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.

Tetramethylammonium bifluoride, crystal structure and vibrational spectra

1989 ◽  
Vol 67 (11) ◽  
pp. 1898-1901 ◽  
Author(s):  
William W. Wilson ◽  
Karl O. Christe ◽  
Jin-an Feng ◽  
Robert Bau
Keyword(s):  
Crystal Structure ◽  
Raman Spectrum ◽  
Vibrational Spectra ◽  
Diffraction Data ◽  
Direct Methods ◽  
X Ray Diffraction ◽  
Orthorhombic Space Group ◽  
X Ray ◽  
Cell Dimensions ◽  
Unit Cell Dimensions

Single crystals of [N(CH3)4]HF2 were obtained as a by-product during the recrystallization of [N(CH3)4]ClF4 from CH3CN solution. X-ray diffraction data show that [N(CH3)4]HF2 crystallizes in the orthorhombic space group Pmn21 with Z = 2 and unit cell dimensions a = 6.611(5), b = 8.753(5), and c = 5.386(4) Å. The structure was solved by direct methods and refined by least squares to a final R = 0.055 by using 205 independent reflections. The HF2− anions are symmetric, exhibit an unusually short [Formula: see text] distance of 2.213(4) Å, and vibrational frequencies close to those of the free HF2− anion. Keywords: tetramethylammonium bifluoride, crystal structure, Raman spectrum.

Crystallization and preliminary X-ray diffraction studies of blasticidin S deaminase from Aspergillus terreus

1999 ◽  
Vol 55 (2) ◽  
pp. 547-548 ◽  
Author(s):  
Masayoshi Nakasako ◽  
Makoto Kimura ◽  
Isamu Yamaguchi
Keyword(s):  
Diffraction Data ◽  
Aspergillus Terreus ◽  
Crystal Structure Analysis ◽  
Thin Plates ◽  
X Ray Diffraction ◽  
Orthorhombic Space Group ◽  
Cell Dimensions ◽  
Crystallization Conditions ◽  
Blasticidin S ◽  
Unit Cell Dimensions

Blasticidin S deaminase from Aspergillus terreus was crystallized with polyethylene glycol 8000. Two types of crystals were grown under the same crystallization conditions. One type grew as thin plates, while the other had a rhombic shape. The rhombic shaped crystal was suitable for high-resolution crystal structure analysis. Precession photographs and diffraction data showed that the crystal belonged to orthorhombic space group P212121, with unit-cell dimensions a = 70.33, b = 146.56 and c = 56.48 Å. The calculated Vm value was acceptable when a tetramer of the enzyme was contained in an asymmetric unit. Preliminary diffraction data were collected to a resolution of 2.0 Å with good statistics.

scholarly journals Crystal structure of uranyl-oxide mineral wölsendorfite revisited

2020 ◽  
Vol 28 (2) ◽  
pp. 322-330
Author(s):  
Jakub Plášil
Keyword(s):  
Crystal Structure ◽  
Structure Refinement ◽  
Complex Structure ◽  
Structural Formula ◽  
X Ray Diffraction ◽  
Orthorhombic Space Group ◽  
X Ray ◽  
Oxide Mineral ◽  
Cell Dimensions ◽  
Unit Cell Dimensions

The crystal structure of the rare supergene Pb2+-containing uranyl-oxide mineral wölsendorfite has been revisited employing the single-crystal X-ray diffraction. The new structure refinement provided deeper insight into the complex structure of this mineral, revealing additional H2O sites in the interlayer complex and confirming the entrance of the Ca2+ into the structure. Studied wölsendorfite is orthorhombic, space group Cmcm, with unit cell dimensions a = 14.1233(8) Å, b = 13.8196(9) Å, c = 55.7953(12) Å, V = 10890.0(10) Å3, and Z = 8. The structure has been refined to an agreement index (R) of 10.74% for 3815 reflections with I > 3σ(I) collected using a microfocus X-ray source from the microcrystal. In line with the previous structure determination, the refined structure contains U–O–OH sheets of the wölsendorfite topology and an interstitial complex comprising nine symmetrically unique Pb sites, occupied dominantly by Pb2+. Nevertheless, one of the sites seems to be plausible for hosting Ca2+. Its presence has been successfully modeled by the refinement and further supported by the crystal-chemical considerations. The structural formula of wölsendorfite crystal studied is Pb6.07Ca0.68[(UO2)14O18(OH)5]O0.5(H2O)12.6, with Z = 8, Dcalc. = 6.919 g·cm–3 (including theoretical 30.2 H atoms). The rather complex structure of wölsendorfite makes it the third most complex known uranyl-oxide hydroxy-hydrate mineral.

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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