scholarly journals Crystallization and preliminary X-ray diffraction studies of guanidinoacetate methyltransferase from rat liver

1999 ◽  
Vol 55 (11) ◽  
pp. 1928-1929 ◽  
Author(s):  
Junichi Komoto ◽  
Yafei Huang ◽  
Yongbo Hu ◽  
Yoshimi Takata ◽  
Kiyoshi Konishi ◽  
...  
Keyword(s):  
Rat Liver ◽  
Unit Cell ◽  
Monoclinic Space Group ◽  
X Ray Diffraction ◽  
Unit Cell Parameters ◽  
Space Group ◽  
X Ray ◽  
Cell Parameters

Guanidinoacetate methyltransferase is the enzyme which catalyzes the last step of creatine biosynthesis. The enzyme is found ubiquitously and in abundance in the livers of all vertebrates. Recombinant rat-liver guanidinoacetate methyltransferase has been crystallized with guanidinoacetate and S-adenosylhomocysteine. The crystals belong to the monoclinic space group P21, with unit-cell parameters a = 54.8, b = 162.5, c = 56.1 Å, β = 96.8 (1)° at 93 K, and typically diffract beyond 2.8 Å.

Molecular and crystal structure of a copper(II) complex of sildenafil

2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Akhmatkhodja N. Yunuskhodjayev ◽  
Shokhista F. Iskandarova ◽  
Vahobjon Kh. Sabirov
Keyword(s):  
Crystal Structure ◽  
Single Crystal ◽  
Unit Cell ◽  
Monoclinic Space Group ◽  
X Ray Diffraction ◽  
Unit Cell Parameters ◽  
Piperazine Ring ◽  
Space Group ◽  
X Ray ◽  
Cell Parameters

Abstract The crystal structure of a copper(II) complex of protonated sildenafil, CuCl3C22H31N6O4S⋅2H2O was studied by single crystal X-ray diffraction. The compound crystallizes in the monoclinic space group P21/n with the unit cell parameters a = 15.4292(2), b = 9.06735(12), c = 21.1752(2) Å, V = 2945.48(7) Å3, Z = 4. The Cu atom is coordinated by the sildenafil ligand via the N2 atom of the pyrazolopyrimidine ring and by three chloride anions. Sildenafil is protonated at the methylated N6 atom of the piperazine ring and it is cation ligand with a 1+ charge.

scholarly journals Crystallization and preliminary X-ray diffraction analysis of the BRPF1 bromodomain in complex with its H2AK5ac and H4K12ac histone-peptide ligands

2014 ◽  
Vol 70 (10) ◽  
pp. 1389-1393 ◽  
Author(s):  
Mulu Y. Lubula ◽  
Amanda Poplawaski ◽  
Karen C. Glass
Keyword(s):  
Diffraction Analysis ◽  
National Laboratory ◽  
Unit Cell ◽  
Monoclinic Space Group ◽  
X Ray Diffraction ◽  
Unit Cell Parameters ◽  
Direct Role ◽  
Space Group ◽  
X Ray ◽  
Cell Parameters

The bromodomain-PHD finger protein 1 (BRPF1) is an essential subunit of the monocytic leukemia zinc (MOZ) histone acetyltransferase (HAT) complex and is required for complex formation and enzymatic activation. BRPF1 contains a structurally conserved bromodomain, which recognizes specific acetyllysine residues on histone proteins. The MOZ HAT plays a direct role in hematopoiesis, and deregulation of its activity is linked to the development of acute myeloid leukemia. However, the molecular mechanism of histone-ligand recognition by the BRPF1 bromodomain is currently unknown. The 117-amino-acid BRPF1 bromodomain was overexpressed inEscherichia coliand purified to homogeneity. Crystallization experiments of the BRPF1 bromodomain in complex with its H4K12ac and H2AK5ac histone ligands yielded crystals that were suitable for high-resolution X-ray diffraction analysis. The BRPF1 bromodomain–H4K12ac crystals belonged to the tetragonal space groupP43212, with unit-cell parametersa= 75.1,b= 75.1,c= 86.3 Å, and diffracted to a resolution of 1.94 Å. The BRPF1 bromodomain–H2AK5ac crystals grew in the monoclinic space groupP21, with unit-cell parametersa= 60.9,b= 55.6,c= 82.1 Å, β = 93.6°, and diffracted to a resolution of 1.80 Å. Complete data sets were collected from both crystal forms using synchrotron radiation on beamline X29 at Brookhaven National Laboratory (BNL).

scholarly journals Chemical Preparation, Crystal Structure Reinvestigation and Vibrational Study of CoNa3P3O10.12H2O and X-ray Characterization of the New Anhydrous Triphosphate CoNa3P3O10

2021 ◽  
Vol 12 (2) ◽  
pp. 2586-2602
Keyword(s):  
Ion Exchange Resin ◽  
Unit Cell ◽  
Monoclinic Space Group ◽  
X Ray Diffraction ◽  
Unit Cell Parameters ◽  
Compound A ◽  
Space Group ◽  
X Ray ◽  
Cell Parameters

The triphosphate dodecahydrate of cobalt and sodium CoNa3P3O10.12H2O was prepared by the ion exchange resin process. Its structure was studied by X-ray diffraction and determined in the monoclinic space group P121/c1with the unit-cell parameters a = 14.6650(5) Å, b=9.1916(3) Å, c = 15.0239(5) Å, =90.2210(10) °, Z = 4 and V = 2025.13(12) Å3. The thermal dehydration of this compound was performed, leading to an anhydrous new form, CoNa3P3O10, which was characterized by X-ray diffraction. The obtained CoNa3P3O10 crystallized in monoclinic space group P21/n with the unit-cell parameters a=15,3774 Å, b=7,6988 A°, c=14,2832A°, β=92,9115°.The characteristic IR wavenumbers of the P3O105− ions observed in the vibrational spectra were calculated using isotopic substitutions, which confirms the existence of these groups in the studied compound. A comparison between the IR and Raman wavenumbers of CoNa3P3O10.12H2O, CoNa3P3O10 and Na5P3O10.12H2O was performed. A kinetic study was also made for CoNa3P3O10·12H2O.

scholarly journals Crystallization and X-ray diffraction analysis of native and selenomethionine-substituted PhyH-DI fromBacillussp. HJB17

2017 ◽  
Vol 73 (11) ◽  
pp. 607-611
Author(s):  
Fang Lu ◽  
Bei Zhang ◽  
Yong Liu ◽  
Ying Song ◽  
Gangxing Guo ◽  
...  
Keyword(s):  
Unit Cell ◽  
Diffusion Method ◽  
Data Sets ◽  
Asymmetric Unit ◽  
X Ray Diffraction ◽  
Unit Cell Parameters ◽  
Solvent Content ◽  
Space Group ◽  
X Ray ◽  
Cell Parameters

Phytases are phosphatases that hydrolyze phytates to less phosphorylatedmyo-inositol derivatives and inorganic phosphate. β-Propeller phytases, which are very diverse phytases with improved thermostability that are active at neutral and alkaline pH and have absolute substrate specificity, are ideal substitutes for other commercial phytases. PhyH-DI, a β-propeller phytase fromBacillussp. HJB17, was found to act synergistically with other single-domain phytases and can increase their efficiency in the hydrolysis of phytate. Crystals of native and selenomethionine-substituted PhyH-DI were obtained using the vapour-diffusion method in a condition consisting of 0.2 Msodium chloride, 0.1 MTris pH 8.5, 25%(w/v) PEG 3350 at 289 K. X-ray diffraction data were collected to 3.00 and 2.70 Å resolution, respectively, at 100 K. Native PhyH-DI crystals belonged to space groupC121, with unit-cell parametersa = 156.84,b = 45.54,c = 97.64 Å, α = 90.00, β = 125.86, γ = 90.00°. The asymmetric unit contained two molecules of PhyH-DI, with a corresponding Matthews coefficient of 2.17 Å3 Da−1and a solvent content of 43.26%. Crystals of selenomethionine-substituted PhyH-DI belonged to space groupC2221, with unit-cell parametersa = 94.71,b= 97.03,c= 69.16 Å, α = β = γ = 90.00°. The asymmetric unit contained one molecule of the protein, with a corresponding Matthews coefficient of 2.44 Å3 Da−1and a solvent content of 49.64%. Initial phases for PhyH-DI were obtained from SeMet SAD data sets. These data will be useful for further studies of the structure–function relationship of PhyH-DI.

The solid solution TbNiIn1−x Ga x

2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Myroslava Horiacha ◽  
Galyna Nychyporuk ◽  
Rainer Pöttgen ◽  
Vasyl Zaremba
Keyword(s):  
Solid Solution ◽  
Unit Cell ◽  
Type Structure ◽  
X Ray Diffraction ◽  
Unit Cell Parameters ◽  
Space Group ◽  
X Ray ◽  
Cell Parameters ◽  
Structure Space ◽  
Arc Melting

Abstract Phase formation in the solid solution TbNiIn1−x Ga x at 873 K was investigated in the full concentration range by means of powder X-ray diffraction and EDX analysis. The samples were synthesized by arc-melting of the pure metals with subsequent annealing at 873 K for one month. The influence of the substitution of indium by gallium on the type of structure and solubility was studied. The solubility ranges have been determined and changes of the unit cell parameters were calculated on the basis of powder X-ray diffraction data: TbNiIn1–0.4Ga0–0.6 (ZrNiAl-type structure, space group P 6 ‾ 2 m $P‾{6}2m$ , a = 0.74461(8)–0.72711(17) and c = 0.37976(5)–0.37469(8) nm); TbNiIn0.2–0Ga0.8–1.0 (TiNiSi-type structure, space group Pnma, а = 0.68950(11)–0.68830(12), b = 0.43053(9)–0.42974(6), с = 0.74186(10)–0.73486(13) nm). The crystal structures of TbNiGa (TiNiSi type, Pnma, a = 0.69140(5), b = 0.43047(7), c = 0.73553(8) nm, wR2=0.0414, 525 F 2 values, 21 variables), TbNiIn0.83(1)Ga0.17(1) (ZrNiAl type, P 6 ‾ 2 m $P‾{6}2m$ , a = 0.74043(6), c = 0.37789(3) nm, wR2 = 0.0293, 322 F 2 values, 16 variables) and TbNiIn0.12(2)Ga0.88(2) (TiNiSi type, Pnma, a = 0.69124(6), b = 0.43134(9), c = 0.74232(11) nm, wR2 = 0.0495, 516 F 2 values, 21 variables) have been determined. The characteristics of the solid solutions and the variations of the unit cell parameters are briefly discussed.

scholarly journals Crystal Chemistry and High-Temperature Behaviour of Ammonium Phases NH4MgCl3·6H2O and (NH4)2Fe3+Cl5·H2O from the Burned Dumps of the Chelyabinsk Coal Basin

Minerals ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 486 ◽  
Author(s):  
Andrey A. Zolotarev ◽  
Elena S. Zhitova ◽  
Maria G. Krzhizhanovskaya ◽  
Mikhail A. Rassomakhin ◽  
Vladimir V. Shilovskikh ◽  
...  
Keyword(s):  
Crystal Structure ◽  
High Temperature ◽  
Unit Cell ◽  
X Ray Diffraction ◽  
Coal Basin ◽  
Unit Cell Parameters ◽  
Space Group ◽  
X Ray ◽  
Cell Parameters ◽  
Mineral Phases

The technogenic mineral phases NH4MgCl3·6H2O and (NH4)2Fe3+Cl5·H2O from the burned dumps of the Chelyabinsk coal basin have been investigated by single-crystal X-ray diffraction, scanning electron microscopy and high-temperature powder X-ray diffraction. The NH4MgCl3·6H2O phase is monoclinic, space group C2/c, unit cell parameters a = 9.3091(9), b = 9.5353(7), c = 13.2941(12) Å, β = 90.089(8)° and V = 1180.05(18) Å3. The crystal structure of NH4MgCl3·6H2O was refined to R1 = 0.078 (wR2 = 0.185) on the basis of 1678 unique reflections. The (NH4)2Fe3+Cl5·H2O phase is orthorhombic, space group Pnma, unit cell parameters a = 13.725(2), b = 9.9365(16), c = 7.0370(11) Å and V = 959.7(3) Å3. The crystal structure of (NH4)2Fe3+Cl5·H2O was refined to R1 = 0.023 (wR2 = 0.066) on the basis of 2256 unique reflections. NH4MgCl3·6H2O is stable up to 90 °C and then transforms to the less hydrated phase isotypic to β-Rb(MnCl3)(H2O)2 (i.e., NH4MgCl3·2H2O), the latter phase being stable up to 150 °C. (NH4)2Fe3+Cl5·H2O is stable up to 120 °C and then transforms to an X-ray amorphous phase. Hydrogen bonds provide an important linkage between the main structural units and play the key role in determining structural stability and physical properties of the studied phases. The mineral phases NH4MgCl3·6H2O and (NH4)2Fe3+Cl5·H2O are isostructural with natural minerals novograblenovite and kremersite, respectively.

scholarly journals Bulachite, [Al6(AsO4)3(OH)9(H2O)4]⋅2H2O from Cap Garonne, France: Crystal structure and formation from a higher hydrate

2020 ◽  
Vol 84 (4) ◽  
pp. 608-615
Author(s):  
Ian E. Grey ◽  
Emre Yoruk ◽  
Stéphanie Kodjikian ◽  
Holger Klein ◽  
Catherine Bougerol ◽  
...  
Keyword(s):  
Unit Cell ◽  
Orthorhombic Symmetry ◽  
X Ray Diffraction ◽  
Unit Cell Parameters ◽  
Space Group ◽  
X Ray ◽  
Cell Parameters ◽  
Different Temperatures ◽  
Using Data ◽  
Hydrated Aluminium

AbstractBulachite specimens from Cap Garonne, France, comprise two intimately mixed hydrated aluminium arsenate minerals with the same Al:As ratio of 2:1 and with different water contents. The crystal structures of both minerals have been solved using data from low-dose electron diffraction tomography combined with synchrotron powder X-ray diffraction. One of the minerals has the same powder X-ray diffraction pattern (PXRD) as for published bulachite. It has orthorhombic symmetry, space group Pnma with unit-cell parameters a = 15.3994(3), b = 17.6598(3), c = 7.8083(1) Å and Z = 4, with the formula [Al6(AsO4)3(OH)9(H2O)4]⋅2H2O. The second mineral is a higher hydrate with composition [Al6(AsO4)3(OH)9(H2O)4]⋅8H2O. It has the same Pnma space group and unit-cell parameters a = 19.855(4), b = 17.6933(11) and c = 7.7799(5) Å i.e. almost the same b and c parameters but a much larger a parameter. The structures are based on polyhedral layers, parallel to (100), of composition [Al6(AsO4)3(OH)9(H2O)4] and with H-bonded H2O between the layers. The layers contain [001] spiral chains of edge-shared octahedra, decorated with corner connected AsO4 tetrahedra that are the same as in the mineral liskeardite. The spiral chains are joined together by octahedral edge-sharing to form layers parallel to (100). Synchrotron PXRD patterns collected at different temperatures during heating of the specimen show that the higher-hydrate mineral starts transforming to bulachite when heated to 50°C, and the transformation is complete between 75 and 100°C.

scholarly journals Cloning, purification, crystallization and preliminary X-ray diffraction of the OleC protein fromStenotrophomonas maltophiliainvolved in head-to-head hydrocarbon biosynthesis

2010 ◽  
Vol 66 (9) ◽  
pp. 1108-1110 ◽  
Author(s):  
Janice A. Frias ◽  
Brandon R. Goblirsch ◽  
Lawrence P. Wackett ◽  
Carrie M. Wilmot
Keyword(s):  
Diffraction Data ◽  
Unit Cell ◽  
Biosynthetic Enzyme ◽  
X Ray Diffraction ◽  
Unit Cell Parameters ◽  
Space Group ◽  
X Ray ◽  
Cell Parameters ◽  
Hydrocarbon Biosynthesis

OleC, a biosynthetic enzyme involved in microbial hydrocarbon biosynthesis, has been crystallized. Synchrotron X-ray diffraction data have been collected to 3.4 Å resolution. The crystals belonged to space groupP3121 orP3221, with unit-cell parametersa=b= 98.8,c= 141.0 Å.

X-ray diffraction data of Ti2O2(C2O4)(OH)2·H2O

1994 ◽  
Vol 9 (3) ◽  
pp. 187-188 ◽  
Author(s):  
Hee-Lack Choi ◽  
Naoya Enomoto ◽  
Nobuo Ishizawa ◽  
Zenbe-e Nakagawa
Keyword(s):  
Powder Diffraction ◽  
Diffraction Data ◽  
Unit Cell ◽  
Powder Diffraction Data ◽  
X Ray Diffraction ◽  
Unit Cell Parameters ◽  
Space Group ◽  
X Ray ◽  
Cell Parameters ◽  
Crystal System

X-ray powder diffraction data for Ti2O2(C2O4)(OH)2·H2O were obtained. The crystal system was determined to be orthorhombic with space group C2221. The unit cell parameters were refined to a = 1.0503(2) nm, b = 1.5509(3) nm, and c = 0.9700(1) nm.

scholarly journals Recombinant expression, purification, crystallization and preliminary X-ray diffraction analysis ofHaemophilus influenzaeBamD and BamCD complex

2015 ◽  
Vol 71 (2) ◽  
pp. 234-238
Author(s):  
Jintang Lei ◽  
Xun Cai ◽  
Xiaodan Ma ◽  
Li Zhang ◽  
Yuwen Li ◽  
...  
Keyword(s):  
Diffraction Analysis ◽  
Recombinant Expression ◽  
Outer Membrane Proteins ◽  
Gel Filtration ◽  
Unit Cell ◽  
X Ray Diffraction ◽  
Unit Cell Parameters ◽  
Space Group ◽  
X Ray ◽  
Cell Parameters

The Bam machinery, which is highly conserved from bacteria to humans, is well recognized as the apparatus responsible for the insertion and folding of most outer membrane proteins in Gram-negative bacteria. InEscherichia coli, the Bam machinery consists of five components (i.e.BamA, BamB, BamC, BamD and BamE). In comparison, there are only four partners inHaemophilus influenzae: a BamB homologue is not found in its genome. In this study, the recombinant expression, purification, crystallization and preliminary X-ray diffraction analysis ofH. influenzaeBamD and BamCD complex are reported. The genes encoding BamC and BamD were cloned into a pET vector and expressed inE. coli. Affinity, ion-exchange and gel-filtration chromatography were used to obtain high-purity protein for further crystallographic characterization. Using the hanging-drop vapour-diffusion technique, BamD and BamCD protein crystals of suitable size were obtained using protein concentrations of 70 and 50 mg ml−1, respectively. Preliminary X-ray diffraction analysis showed that the BamD crystals diffracted to 4.0 Å resolution and belonged to space groupP212121, with unit-cell parametersa= 54.5,b= 130.5,c= 154.7 Å. The BamCD crystals diffracted to 3.8 Å resolution and belonged to space groupI212121, with unit-cell parametersa= 101.6,b= 114.1,c= 234.9 Å.

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