Crystallization and preliminary analysis of bovine adenosine deaminase

1999 ◽  
Vol 55 (12) ◽  
pp. 2031-2032 ◽  
Author(s):  
Takayoshi Kinoshita ◽  
Nobuya Nishio ◽  
Akihiro Sato ◽  
Masayoshi Murata
Keyword(s):  
Adenosine Deaminase ◽  
Ammonium Sulfate ◽  
Preliminary Analysis ◽  
Unit Cell ◽  
Molecular Replacement ◽  
Unit Cell Parameters ◽  
Space Group ◽  
Cell Parameters ◽  
Vapour Diffusion

Adenosine deaminase (ADA) from bovine intestine was crystallized with purine riboside by vapour diffusion using ammonium sulfate as precipitant. The crystals are tetragonal and have unit-cell parameters a = b = 80.03, c = 141.68 Å. They belong to space group P41212 or P43212 and diffract to at least 2.0 Å resolution. The structure is being solved by molecular replacement.

scholarly journals Purification, crystallization and initial crystallographic analysis of the α-catenin homologue HMP-1 fromCaenorhabditis elegans

2016 ◽  
Vol 72 (3) ◽  
pp. 234-239 ◽  
Author(s):  
Hyunook Kang ◽  
Injin Bang ◽  
William I. Weis ◽  
Hee-Jung Choi
Keyword(s):  
Crystallographic Analysis ◽  
Unit Cell ◽  
Molecular Replacement ◽  
Binding Region ◽  
Unit Cell Parameters ◽  
Mechanical Tension ◽  
Space Group ◽  
Cell Parameters ◽  
Terminal Domain ◽  
Mammalian Homologue

Adherens junctions transmit mechanical force between cells. In these junctions, β-catenin binds to cadherins and to the N-terminal domain of α-catenin, which in turn binds to actin filamentsviaits C-terminal domain. The middle (M) domain of α-catenin plays an important role in responding to mechanical tension. The nematodeCaenorhabditis eleganscontains α- and β-catenin homologues called HMP-1 and HMP-2, respectively, but HMP-1 behaves differently from its mammalian homologue. Thus, structural and biochemical studies of HMP-1 have been initiated to understand the mechanism of HMP-1 and the evolution of α-catenin. The N-terminal domain of HMP-1 in complex with the minimal HMP-1-binding region of HMP-2 was purified and crystallized. These crystals diffracted to 1.6 Å resolution and belonged to space groupP3121, with unit-cell parametersa=b= 57.1,c= 155.4 Å. The M domain of HMP-1 was also purified and crystallized. The M-domain crystals diffracted to 2.4 Å resolution and belonged to space groupP212121, with unit-cell parametersa = 72.8,b= 81.5,c = 151.4 Å. Diffraction data were collected and processed from each crystal, and the structures were solved by molecular replacement.

scholarly journals Purification, crystallization and preliminary X-ray crystallographic studies of Rv3705c fromMycobacterium tuberculosis

2014 ◽  
Vol 70 (8) ◽  
pp. 1090-1092
Author(s):  
Feifei Lu ◽  
Feng Gao ◽  
Honglin Li ◽  
Weimin Gong ◽  
Lin Zhou ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Unit Cell ◽  
Diffusion Method ◽  
Unit Cell Parameters ◽  
Space Group ◽  
X Ray ◽  
Cell Parameters ◽  
Vapour Diffusion

The conserved protein Rv3705c fromMycobacterium tuberculosishas been cloned, expressed, purified and crystallized by the sitting-drop vapour-diffusion method using PEG 3350 as a precipitant. The Rv3705c crystals exhibited space groupP6122 orP6522, with unit-cell parametersa=b= 198.0,c= 364.1 Å, α = β = 90, γ = 120°, and diffracted to a resolution of 3.3 Å.

Crystallization of Pleurotus ostreatus (oyster mushroom) lectin

1999 ◽  
Vol 55 (9) ◽  
pp. 1589-1590 ◽  
Author(s):  
T. K. Chattopadhyay ◽  
J. N. Lisgarten ◽  
R. Brechtel ◽  
H. Rüdiger ◽  
R. A. Palmer
Keyword(s):  
Ammonium Sulfate ◽  
Pleurotus Ostreatus ◽  
Unit Cell ◽  
Oyster Mushroom ◽  
Hanging Drop ◽  
Unit Cell Parameters ◽  
Space Group ◽  
Cell Parameters ◽  
Drop Technique ◽  
Mushroom Lectin

Crystals of Pleurotus ostreatus (oyster mushroom) lectin have been grown by the hanging-drop technique using ammonium sulfate as the precipitant at 293 K. Over a period of between two and three weeks, crystals of hexagonal bipyramidal morphology grew to maximum dimensions of 0.2 × 0.2 × 0.5 mm. The crystals belong to space group P6122 or P6522, with unit-cell parameters a = b = 155.9, c = 149.8 Å, V = 3153078 Å3, Z = 12 (assuming 50% solvent), and diffract to 4.1 Å at 293 K.

Crystallization of the catalytic domain of Clostridium cellulolyticum CeIF cellulase in the presence of a newly synthesized cellulase inhibitor

1998 ◽  
Vol 54 (1) ◽  
pp. 114-118 ◽  
Author(s):  
Corinne Reverbel-Leroy ◽  
Goetz Parsiegla ◽  
Vincent Moreau ◽  
Michel Juy ◽  
Chantal Tardif ◽  
...  
Keyword(s):  
Catalytic Domain ◽  
Glycosyl Hydrolase ◽  
Unit Cell ◽  
Unit Cell Parameters ◽  
Space Group ◽  
Cell Parameters ◽  
Clostridium Cellulolyticum ◽  
Vapour Diffusion

The catalytic domain of the CeIF processive endocellulase, a family 48 glycosyl hydrolase from Clostridium cellulolyticum has been crystallized in the presence of a newly synthesized inhibitor (methyl 4-S-β-cellobiosyl-4-thio-β-cellobioside), by vapour diffusion, using PEG as a precipitant. The protein crystallizes in the orthorhombic P212121 space group and diffracts to a resolution of 2.0 Å. The unit-cell parameters are a = 61.4, b = 84.5, c = 121.9 Å.

Expression, purification, crystallization and preliminary X-ray analysis of the κ-carrageenase from Pseudoalteromonas carrageenovora

1999 ◽  
Vol 55 (4) ◽  
pp. 918-920 ◽  
Author(s):  
Gurvan Michel ◽  
Tristan Barbeyron ◽  
Didier Flament ◽  
Thierry Vernet ◽  
Bernard Kloareg ◽  
...  
Keyword(s):  
Polyethylene Glycol ◽  
Unit Cell ◽  
Recombinant Form ◽  
Diffusion Method ◽  
Unit Cell Parameters ◽  
Space Group ◽  
X Ray ◽  
Cell Parameters ◽  
Vapour Diffusion

A recombinant form of His-tagged κ-carrageenase from Pseudoalteromonas carrageenovora has been expressed, purified and crystallized. Crystals have been obtained by the vapour-diffusion method using polyethylene glycol (Mr = 4000) as a precipitant. These crystals belong to the space group P212121, with unit-cell parameters a  =  58.2, b  =  62.8, c  =  77.9 Å, and diffract to 2.2 Å resolution on a rotating-anode X-ray source.

scholarly journals The novel thermostable cellulose-degrading enzyme DtCel5H from Dictyoglomus thermophilum: crystallization and X-ray crystallographic analysis

2018 ◽  
Vol 74 (1) ◽  
pp. 1-5
Author(s):  
Flavia Squeglia ◽  
Rita Berisio ◽  
Alessia Ruggiero
Keyword(s):  
Ammonium Sulfate ◽  
Glycosyl Hydrolase ◽  
Unit Cell ◽  
Structure Stability ◽  
Waste Biomass ◽  
Unit Cell Parameters ◽  
Orthorhombic Space Group ◽  
Space Group ◽  
Cell Parameters ◽  
Dictyoglomus Thermophilum

Cellulose-based products constitute the great majority of municipal waste, and applications of cellulases in the conversion of waste biomass to biofuels will be a key technology in future biorefineries. Currently, multi-enzymatic pre-treatment of biomass is a crucial step in making carbohydrates more accessible for subsequent fermentation. Using bioinformatics analysis, endo-β-(1,4)-glucanase from Dictyoglomus thermophilum (DtCel5H) was identified as a new member of glycosyl hydrolase family 5. The gene encoding DtCel5H was cloned and the recombinant protein was overexpressed for crystallization and biophysical studies. Here, it is shown that this enzyme is active on cellulose substrates and is highly thermostable. Crystals suitable for crystallographic investigations were also obtained in different crystallization conditions. In particular, ordered crystals of DtCel5H were obtained using either ammonium sulfate or polyethylene glycol (PEG) as a precipitant agent. The crystals obtained in the presence of ammonium sulfate belonged to space group P32, with unit-cell parameters a = 73.1, b = 73.1, 73.1, c = 127.8 Å, and diffracted to 1.5 Å resolution, whereas the second crystal form belonged to the orthorhombic space group P212121, with unit-cell parameters a = 49.3, b = 67.9, c = 103.7 Å, and diffracted to 1.6 Å resolution. The crystal structure was solved in both space groups using molecular-replacement methods. Structure–activity and structure–stability studies of DtCel5H will provide insights for the design of high-performance enzymes.

Crystallization and preliminary crystal analysis of yeast hexokinase PI and PII

1999 ◽  
Vol 55 (12) ◽  
pp. 2047-2048 ◽  
Author(s):  
Paula R. Kuser ◽  
Alexander M. Golubev ◽  
Igor Polikarpov
Keyword(s):  
Signal Transduction ◽  
Unit Cell ◽  
Hanging Drop ◽  
Synchrotron Diffraction ◽  
Unit Cell Parameters ◽  
Space Group ◽  
Cell Parameters ◽  
Vapour Diffusion ◽  
Hanging Drop Method ◽  
Yeast Hexokinase

Hexokinase is the prime enzyme of the Embden–Meyerhof pathway and is responsible for the first stage of energy conversion. It catalyzes the transfer of a phosphate to glucose to form glucose-6-phosphate. Yeast hexokinase PII is also known to play an important role in glucose signal transduction. Crystals of yeast hexokinase isoforms PI and PII were obtained by vapour-diffusion techniques using the hanging-drop method. Isoform PI crystals belong to the space group P212121, with unit-cell parameters a = 62.12, b = 78.87, c = 144.74 Å. Unit-cell parameters for isoform PII crystals are a = b = 142.81, c = 58.46 Å and the space group is I4. Synchrotron diffraction data have been collected to 2.2 Å resolution from the isoform PII crystal, whereas isoform PI diffracted to 3.1 Å.

scholarly journals Crystallization and X-ray analysis of the extracellular adhesion domain ofHelicobacter pyloriadhesin A: the significance of the cation composition in the crystallization precipitant

2017 ◽  
Vol 73 (4) ◽  
pp. 202-208 ◽  
Author(s):  
Ling Guo ◽  
Jinyong Zhang ◽  
Liwei Cui ◽  
Dong Liu ◽  
Bo Ma ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Ammonium Sulfate ◽  
Unit Cell ◽  
Host Cells ◽  
Lithium Sulfate ◽  
Unit Cell Parameters ◽  
Data Set ◽  
Space Group ◽  
X Ray ◽  
Cell Parameters

Adherence to host cells is a crucial step in the process of bacterial infection, which is usually mediated by a number of outer membrane proteins identified as adhesins.Helicobacter pyloriadhesin A (HpaA) is a member of the adhesin family that mediates the adherence ofHelicobacter pylorito gastric epithelial cells, and consequently assists the bacteria in becoming a life-long colonizer of the human stomach. In this study, two constructs were made for the production of truncated HpaA proteins comprising residues 31–260 and 53–260, respectively. The products of both constructs were crystallized, but only the protein from the shorter construct (residues 53–260) formed crystals that were capable of diffraction. In the subsequent optimization trials, crystals in different forms were unexpectedly obtained by using lithium sulfate and ammonium sulfate as the precipitant. An X-ray data set was collected to 1.95 Å resolution on beamline BL18U1 at SSRF using a crystal grown with 1.92 Mlithium sulfate, which belonged to space groupP65with unit-cell parametersa=b= 95.42,c = 54.72 Å, γ = 120°, while another crystal grown with 1.9 Mammonium sulfate diffracted to 2.60 Å resolution and the collected data set was indexed in space groupP21212, with unit-cell parametersa= 121.01,b= 190.56,c= 106.31 Å. The collection of diffraction data has established a solid basis for structure determination.

scholarly journals Structure of the kinase domain of Gilgamesh fromDrosophila melanogaster

2014 ◽  
Vol 70 (4) ◽  
pp. 438-443 ◽  
Author(s):  
Ni Han ◽  
CuiCui Chen ◽  
Zhubing Shi ◽  
Dianlin Cheng
Keyword(s):  
Kinase Domain ◽  
Unit Cell ◽  
Molecular Replacement ◽  
Active Conformation ◽  
Structural Comparison ◽  
Unit Cell Parameters ◽  
Hedgehog Signalling ◽  
Space Group ◽  
Cell Parameters ◽  
And Function

The CK1 family kinases regulate multiple cellular aspects and play important roles in Wnt/Wingless and Hedgehog signalling. The kinase domain ofDrosophilaGilgamesh isoform I (Gilgamesh-I), a homologue of human CK1-γ, was purified and crystallized. Crystals of methylated Gilgamesh-I kinase domain with a D210A mutation diffracted to 2.85 Å resolution and belonged to space groupP43212, with unit-cell parametersa=b= 52.025,c= 291.727 Å. The structure of Gilgamesh-I kinase domain, which was determined by molecular replacement, has conserved catalytic elements and an active conformation. Structural comparison indicates that an extended loop between the α1 helix and the β4 strand exists in the Gilgamesh-I kinase domain. This extended loop may regulate the activity and function of Gilgamesh-I.

Crystallization and preliminary X-ray studies on the molbindin ModG from Azotobacter vinelandii

1999 ◽  
Vol 55 (7) ◽  
pp. 1356-1358 ◽  
Author(s):  
Clare E. M. Williams ◽  
Daniel J. White ◽  
Laure Delarbre ◽  
Lesley A. Mitchenall ◽  
Richard N. Pau ◽  
...  
Keyword(s):  
Marked Improvement ◽  
Azotobacter Vinelandii ◽  
Unit Cell ◽  
Unit Cell Parameters ◽  
Space Group ◽  
X Ray ◽  
Cell Parameters ◽  
Cell Dimensions ◽  
Vapour Diffusion ◽  
Unit Cell Dimensions

Crystals of the molbindin ModG (subunit Mr = 14359 Da), a cytoplasmic molybdate-binding protein from Azotobacter vinelandii, were grown by vapour diffusion. Both apo and tungstate-bound forms were crystallized and X-ray data were collected at 100 K. Apo-ModG crystallizes in space group P6322, with unit-cell dimensions a = b = 90.62, c = 79.46 Å. Native data to a resolution of 2.5 Å were collected from a single crystal, which showed a marked improvement in diffraction quality after annealing. Data from a single-site gold derivative were also collected at 2.7 Å resolution. Crystals of the ligand-bound form of ModG belong to space group P321, with unit-cell parameters a = b = 50.57, c = 79.29 Å. X-ray data to a resolution of 2.0 Å were collected.

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