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.

Crystallization and preliminary X-ray diffraction studies of piratoxin III, a D-49 phospholipase A2 from the venom of Bothrops pirajai

1999 ◽  
Vol 55 (6) ◽  
pp. 1229-1230 ◽  
Author(s):  
Lee Wen-Hwa ◽  
Marcos H. Toyama ◽  
Andreimar M. Soares ◽  
José R. Giglio ◽  
Sérgio Marangoni ◽  
...  
Keyword(s):  
Search Model ◽  
Molecular Replacement ◽  
X Ray Diffraction ◽  
Unit Cell Parameters ◽  
X Ray ◽  
Cell Parameters ◽  
Diffusion Technique ◽  
Vapour Diffusion ◽  
Replacement Solution ◽  
Bothrops Pirajai

Piratoxin III (PrTX-III) is a phospholipase A2 (PLA2, E.C. 3.1.1.4, phosphatide sn-2 acylhydrolase) isolated from Bothrops pirajai. Crystals of PrTX-III were obtained using the vapour-diffusion technique and X-ray diffraction data have been collected to 2.7 Å resolution. The enzyme was crystallized in the space group C2 with unit-cell parameters a = 60.88, b = 100.75, c = 48.19 Å, β = 123.89°. A molecular-replacement solution of the structure has been found using bothropstoxin I from the venom of B. jararacussu as a search model.

Crystallization and preliminary X-ray diffraction studies of piratoxin II, a phospholipase A2 isolated from the venom of Bothrops pirajai

1998 ◽  
Vol 54 (6) ◽  
pp. 1437-1439
Author(s):  
W.-H. Lee ◽  
M. C. Gonçalez ◽  
R. M. F. Ramalheira ◽  
P. R. Kuser ◽  
M. H. Toyama ◽  
...  
Keyword(s):  
Crystallographic Structure ◽  
Search Model ◽  
Molecular Replacement ◽  
X Ray Diffraction ◽  
X Ray ◽  
Cell Parameters ◽  
Diffusion Technique ◽  
Bothrops Asper ◽  
Bothrops Pirajai ◽  
Phospholipases A

The phospholipases A2 (PLA2, E.C. 3.1.1.4, phosphatide sn2 acylhydrolases) are the major components of the venom of several snakes. They are responsible for several important pharmacological effects observed in ophidian incidents. PLA2 piratoxin II from Bothrops pirajai has been crystallized by the vapour-diffusion technique. X-ray diffraction data have been collected to 2.04 Å resolution (90.2% complete, R merge = 0.070). The space group is P21 and the cell parameters are a = 46.19, b = 60.36, c = 58.74 Å and β = 96.05°. The structure has been solved by molecular replacement using the crystallographic structure of PLA2 from Bothrops asper (PDB code 1CLP) as a search model.

The structure of plastocyanin from the cyanobacterium Phormidium laminosum

1999 ◽  
Vol 55 (2) ◽  
pp. 414-421 ◽  
Author(s):  
Charles S. Bond ◽  
Derek S. Bendall ◽  
Hans C. Freeman ◽  
J. Mitchell Guss ◽  
Christopher J. Howe ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Search Model ◽  
Molecular Replacement ◽  
Amino Acid Residues ◽  
Asymmetric Unit ◽  
Threefold Axis ◽  
Phormidium Laminosum ◽  
X Ray ◽  
Cell Dimensions ◽  
Unit Cell Dimensions

The crystal structure of the `blue' copper protein plastocyanin from the cyanobacterium Phormidium laminosum has been solved and refined using 2.8 Å X-ray data. P. laminosum plastocyanin crystallizes in space group P43212 with unit-cell dimensions a = 86.57, c = 91.47 Å and with three protein molecules per asymmetric unit. The final residual R is 19.9%. The structure was solved using molecular replacement with a search model based on the crystal structure of a close homologue, Anabaena variabilis plastocyanin (66% sequence identity). The molecule of P. laminosum plastocyanin has 105 amino-acid residues. The single Cu atom is coordinated by the same residues – two histidines, a cysteine and a methionine – as in other plastocyanins. In the crystal structure, the three molecules of the asymmetric unit are related by a non-crystallographic threefold axis. A Zn atom lies between each pair of neighbouring molecules in this ensemble, being coordinated by a surface histidine residue of one molecule and by two aspartates of the other.

The high-pressure cadmium borate Cd6B22O39·H2O

2015 ◽  
Vol 70 (3) ◽  
pp. 183-190 ◽  
Author(s):  
Gerhard Sohr ◽  
Nina Ciaghi ◽  
Klaus Wurst ◽  
Hubert Huppertz
Keyword(s):  
High Pressure ◽  
High Temperature ◽  
Structural Characteristics ◽  
X Ray Diffraction ◽  
X Ray ◽  
High Pressure High Temperature ◽  
Cell Dimensions ◽  
Temperature Experiment ◽  
Unit Cell Dimensions ◽  
Ir And Raman

AbstractSingle crystals of the hydrous cadmium borate Cd6B22O39·H2O were obtained through a high-pressure/high-temperature experiment at 4.7 GPa and 1000 °C using a Walker-type multianvil apparatus. CdO and partially hydrolyzed B2O3 were used as starting materials. A single crystal X-ray diffraction study has revealed that the structure of Cd6B22O39·H2O is similar to that of the type M6B22O39·H2O (M=Fe, Co). Layers of corner-sharing BO4 groups are interconnected by BO3 groups to form channels containing the metal cations, which are six- and eight-fold coordinated by oxygen atoms. The compound crystallizes in the space group Pnma (no. 62) [R1=0.0379, wR2=0.0552 (all data)] with the unit cell dimensions a=1837.79(5), b=777.92(2), c=819.08(3) pm, and V=1171.00(6) Å3. The IR and Raman spectra reflect the structural characteristics of Cd6B22O39·H2O.

scholarly journals X-ray crystal structure of a malonate-semialdehyde dehydrogenase fromPseudomonassp. strain AAC

2017 ◽  
Vol 73 (1) ◽  
pp. 24-28 ◽  
Author(s):  
Matthew Wilding ◽  
Colin Scott ◽  
Thomas S. Peat ◽  
Janet Newman
Keyword(s):  
Crystal Structure ◽  
Search Model ◽  
Molecular Replacement ◽  
X Rays ◽  
X Ray Diffraction ◽  
Acetyl Coa ◽  
Space Group ◽  
X Ray ◽  
Semialdehyde Dehydrogenase

The NAD-dependent malonate-semialdehyde dehydrogenase KES23460 fromPseudomonassp. strain AAC makes up half of a bicistronic operon responsible for β-alanine catabolism to produce acetyl-CoA. The KES23460 protein has been heterologously expressed, purified and used to generate crystals suitable for X-ray diffraction studies. The crystals belonged to space groupP212121and diffracted X-rays to beyond 3 Å resolution using the microfocus beamline of the Australian Synchrotron. The structure was solved using molecular replacement, with a monomer from PDB entry 4zz7 as the search model.

X–Ray Powder Diffraction Data for Synthetic Varieties of Tetrahedrite

1991 ◽  
Vol 6 (1) ◽  
pp. 43-47 ◽  
Author(s):  
Neil E. Johnson
Keyword(s):  
Powder Diffraction ◽  
Experimental Unit ◽  
Regression Equations ◽  
Powder Diffraction Data ◽  
X Ray Diffraction ◽  
X Ray ◽  
Validation Test ◽  
Cell Dimensions ◽  
Synthetic Varieties ◽  
Unit Cell Dimensions

AbstractA series of five synthetic tetrahedrite-group minerals has been prepared and examined using powder X-ray diffraction in order to update current powder data and provide a validation test of cell dimension prediction equations. The tetrahedrites (nominally (Cu10X2)Sb4S13 with X = Zn, Cd, Mn, Hg and Fe) have the following properties: zincian tetrahedrite, a = 10.3833 (1) Å, Dx = 4.974 (1) g/cm3, F30 = 264 (0.004, 31), M20 = 279; cadmian tetrahedrite, a = 10.5066 (1) Å, Dx = 5.073 (1) g/cm3, F30 = 208 (0.004, 37), M20 = 249; manganoan tetrahedrite, a = 10.4384 (1) Å, Dx = 4.822 (1) g/cm3, F30 = 274 (0.003, 33), M20 = 302; mercurian tetrahedrite, a = 10.5071 (1) Å, Dx = 5.570 (1) g/cm3, F30 = 150 (0.006, 35), M20 = 156; ferroan tetrahedrite, a = 10.3630 (1) Å, Dx = 5.002 (1) g/cm3, F30 = 253 (0.004, 33), M20 = 281. The experimental unit cell dimensions obtained in this study are in excellent agreement with calculated values produced using regression equations developed previously.

Powder X-Ray Diffraction Data for Ca2Bi2O5and C4Bi6O13

1992 ◽  
Vol 7 (2) ◽  
pp. 109-111 ◽  
Author(s):  
C.J. Rawn ◽  
R.S. Roth ◽  
H.F. McMurdie
Keyword(s):  
Powder Diffraction ◽  
Diffraction Data ◽  
Neutron Powder Diffraction ◽  
X Ray Diffraction ◽  
Space Group ◽  
X Ray ◽  
Cell Dimensions ◽  
Powder Samples ◽  
Orthorhombic Cell ◽  
Unit Cell Dimensions

AbstractSingle crystals and powder samples of Ca2Bi5O5and Ca4Bi6O13have been synthesized and studied using single crystal X-ray diffraction as well as X-ray and neutron powder diffraction. Unit cell dimensions were calculated using a least squares analysis that refined to a δ2θof no more than 0.03°. A triclinic cell was found with space group , a = 10.1222(7), b = 10.1466(6), c = 10.4833(7) Å. α= 116.912(5), β= 107.135(6) and γ= 92.939(6)°, Z = 6 for the Ca2Bi2O5compound. An orthorhombic cell was found with space group C2mm, a = 17.3795(5), b = 5.9419(2) and c = 7.2306(2) Å, Z = 2 for the Ca4Bi6O13compound.

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.

scholarly journals An examination of the thermal expansion of urea using high-resolution variable-temperature X-ray powder diffraction

2005 ◽  
Vol 38 (6) ◽  
pp. 1038-1039 ◽  
Author(s):  
Robert Hammond ◽  
Klimentina Pencheva ◽  
Kevin J. Roberts ◽  
Patricia Mougin ◽  
Derek Wilkinson
Keyword(s):  
Thermal Expansion ◽  
High Resolution ◽  
Variable Temperature ◽  
X Ray Diffraction ◽  
Polymorphic Transformations ◽  
X Ray ◽  
Thermal Expansion Coefficients ◽  
Cell Dimensions ◽  
Expansion Coefficients ◽  
Unit Cell Dimensions

Variable-temperature high-resolution capillary-mode powder X-ray diffraction is used to assess changes in unit-cell dimensions as a function of temperature over the range 188–328 K. No evidence was found for any polymorphic transformations over this temperature range and thermal expansion coefficients for urea were found to be αa= (5.27 ± 0.26) × 10−5 K−1and αc= (1.14 ± 0.057) × 10−5 K−1.

Powder X-ray diffraction data for Ba4ZnTi11O27 and Ba2ZnTi5O13

1994 ◽  
Vol 9 (1) ◽  
pp. 56-62 ◽  
Author(s):  
C. G. Lindsay ◽  
C. J. Rawn ◽  
R. S. Roth
Keyword(s):  
Single Crystal ◽  
Single Crystals ◽  
Powder Diffraction ◽  
Diffraction Data ◽  
Lattice Parameters ◽  
X Ray Diffraction ◽  
X Ray ◽  
Cell Dimensions ◽  
Powder Samples ◽  
Unit Cell Dimensions

Single crystals and powder samples of Ba4ZnTi11O27 and Ba2ZnTi5O13 have been synthesized and studied using single-crystal X-ray precession photographs and X-ray powder diffraction. Unit cell dimensions were calculated from a least-squares refinement with a final maximum Δ2θ of 0.05°. Both phases were found to have monoclinic cells, space group C2/m. The refined lattice parameters for the Ba4ZnTi11O27 compound are a= 19.8687(8) Å, b=11.4674(5) Å, c=9.9184(4) Å, β= 109.223(4)°, and Z=4. The refined lattice parameters for the Ba2ZnTi5O13 compound are a= 15.2822(7) Å, b=3.8977(1) Å, c=9.1398(3) Å, β=98.769(4)°, and Z=2.

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