Crystallization and preliminary X-ray analysis of the Escherichia coli UDP-MurNAc-tripeptide D-alanyl-D-alanine-adding enzyme (MurF)

1999 ◽  
Vol 55 (12) ◽  
pp. 2033-2034 ◽  
Author(s):  
Youwei Yan ◽  
Sanjeev Munshi ◽  
Ying Li ◽  
Kelly Ann D. Pryor ◽  
Frank Marsilio ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Asymmetric Unit ◽  
Hanging Drop ◽  
Data Set ◽  
Solvent Content ◽  
X Ray ◽  
Protein Mass ◽  
Cell Dimensions ◽  
Unit Cell Dimensions ◽  
Crystal Volume

Crystals of the Escherichia coli UDP-MurNAc-tripeptide D-Ala-D-Ala-adding protein (MurF), which catalyzes the formation of the last metabolite of the bacterial cell-wall building block, have been grown in hanging-drop vapor-diffusion trials using PEG 8K as a precipitating agent. The crystals belong to hexagonal space group P61 or P65, with unit-cell dimensions a = b = 74, c = 425 Å. The asymmetric unit contains two molecules, with a crystal volume per protein mass (Vm ) of 3.4 Å3 Da−1 and a solvent content of about 64% by volume. A native data set to 2.8 Å resolution has been obtained from a frozen crystal using a synchrotron X-ray source.

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 diffraction analysis of the HincII restriction endonuclease–DNA complex

1999 ◽  
Vol 55 (11) ◽  
pp. 1943-1945 ◽  
Author(s):  
Nancy C. Horton ◽  
Lydia F. Dorner ◽  
Ira Schildkraut ◽  
John J. Perona
Keyword(s):  
High Energy ◽  
Asymmetric Unit ◽  
Hanging Drop ◽  
Data Set ◽  
Synchrotron Source ◽  
Polyethylene Glycol 4000 ◽  
Dimeric Complexes ◽  
Cell Dimensions ◽  
Unit Cell Dimensions ◽  
Dna Complex

Crystals of the 60 kDa dimeric HincII restriction enzyme bound to a 12 base-pair dyad-symmetric duplex DNA carrying the specific 5′-GTCGAC recognition site have been obtained. Crystals grew by hanging-drop vapor diffusion from solutions containing polyethylene glycol 4000 as precipitating agent. The rod-shaped crystals belong to space group I222 (or I212121), with unit-cell dimensions a = 66.9, b = 176.7, c = 256.0 Å. There are most likely to be two dimeric complexes in the asymmetric unit. A complete native data set has been collected from a high-energy synchrotron source to a resolution of 2.5 Å at 100 K, with an R merge of 4.8%.

Crystallization and preliminary X-ray studies of β-1,4-galactanase from Aspergillus aculeatus

1999 ◽  
Vol 55 (4) ◽  
pp. 929-930 ◽  
Author(s):  
C. Ryttersgaard ◽  
J.-C. N. Poulsen ◽  
S. Christgau ◽  
T. Sandal ◽  
H. Dalbøge ◽  
...  
Keyword(s):  
Asymmetric Unit ◽  
X Ray Diffraction ◽  
Aspergillus Aculeatus ◽  
Solvent Content ◽  
X Ray ◽  
Space Groups ◽  
Peg 400 ◽  
Cell Dimensions ◽  
Vapour Diffusion ◽  
Unit Cell Dimensions

Recombinant β-1,4-galactanase from Aspergillus aculeatus has been crystallized and characterized by X-ray diffraction. Crystals were obtained in hanging drops by vapour-diffusion under the conditions 30% PEG 400, 0.2 M CaCl2 and 0.1 M Na HEPES buffered to pH 7.5. The crystals diffract to 2.3 Å resolution and belong to one of the orthorhombic space groups I222 or I212121. The unit-cell dimensions are a = 60.42, b = 88.94 and c = 129.08 Å. With one molecule in the asymmetric unit, the corresponding solvent content is ∼48%.

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.

Crystallization and preliminary X-ray investigation of the complex of RNase Sa with wild-type barstar

1998 ◽  
Vol 54 (3) ◽  
pp. 403-404 ◽  
Author(s):  
Lubica Urbanikova ◽  
Jozef Sevcik
Keyword(s):  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Asymmetric Unit ◽  
Wild Type ◽  
Protein Inhibitor ◽  
Hanging Drop ◽  
X Ray ◽  
Natural Protein ◽  
Cell Dimensions ◽  
Unit Cell Dimensions

RNase Sa, an extracellular ribonuclease produced by Streptomyces aureofaciens, is inhibited by barstar, the natural protein inhibitor of barnase, the ribonuclease of Bacillus amyloliquefaciens. The complex of RNase Sa with wild-type barstar was crystallized by hanging-drop vapour diffusion. It was shown by sodium dodecyl sulfate polyacrylamide gel electrophoresis that RNase Sa and barstar are present in equimolar proportions in the crystals. The crystals are in the hexagonal space group P65 with unit cell dimensions a = b = 56.95, c = 135.8 Å. They diffract to 1.7 Å resolution at the DESY synchronton source. The asymmetric unit contains one molecule of the complex.

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 studies of hORF6, a novel human antioxidant enzyme

1998 ◽  
Vol 54 (3) ◽  
pp. 436-436 ◽  
Author(s):  
Hee-Jeong Choi ◽  
Sang Won Kang ◽  
Chul-Hak Yang ◽  
Sue Goo Rhee ◽  
Seong-Eon Ryu
Keyword(s):  
Antioxidant Enzyme ◽  
Unit Cell ◽  
X Rays ◽  
Asymmetric Unit ◽  
Data Set ◽  
X Ray ◽  
Space Groups ◽  
Cell Dimensions ◽  
Hanging Drop Method ◽  
Unit Cell Dimensions

HORF6 is a member of the novel antioxidant enzyme family found in humans. A recombinant form of hORF6 expressed and purified from E. coli has been crystallized by the hanging-drop method using various PEG's as precipitating agents. HORF6 crystallizes in two different monoclinic space groups, P21 and C2. The P21 crystals have unit-cell dimensions of a = 47.85, b = 75.17, c = 63.30 Å and β = 110.21° and contain two monomers per asymmetric unit, while the C2 crystals have unit-cell dimensions of a = 165.27, b = 95.44, c = 166.44 Å and β = 128.97° and contain more than six monomers per asymmetric unit. The P21 crystals with the smaller unit cell diffract X-rays better and behave well for the X-ray analysis. A native data set from a single crystal of the P21 space group gas been collected to 2.0 Å resolution.

Crystallization and preliminary X-ray studies of the Rhizobium meliloti DctD two-component receiver domain

1998 ◽  
Vol 54 (6) ◽  
pp. 1416-1418
Author(s):  
Mark Staley ◽  
Lori C. Zeringue ◽  
Richard D. Kidd ◽  
B. Tracy Nixon ◽  
Gregory K. Farber
Keyword(s):  
Rhizobium Meliloti ◽  
Ammonium Phosphate ◽  
Asymmetric Unit ◽  
Hanging Drop ◽  
X Ray ◽  
Diffusion Geometry ◽  
Receiver Domain ◽  
Cell Dimensions ◽  
Two Component ◽  
Unit Cell Dimensions

The Rhizobium meliloti DctD two-component receiver domain was expressed in Escherichia coli and purified to homogeneity. Crystals were obtained using the hanging-drop vapor-diffusion geometry with ammonium phosphate as the precipitant. The crystals diffract to 2.3 Å and exhibit the symmetry of space group I222 or I212121. The unit-cell dimensions are a = 59.0, b = 58.6 and c = 169.8 Å. The asymmetric unit contains a dimer and the crystals have a Vm of 2.16 Å3 Da−1.

The FNR-like domain of the Escherichia coli sulfite reductase flavoprotein component: crystallization and preliminary X-ray analysis

1998 ◽  
Vol 54 (1) ◽  
pp. 135-136 ◽  
Author(s):  
Arnaud Gruez ◽  
Mahel Zeghouf ◽  
Jay Bertrand ◽  
Michel Eschenbrenner ◽  
Jacques Covès ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Sulfite Reductase ◽  
Asymmetric Unit ◽  
Hanging Drop ◽  
Unit Cell Parameters ◽  
Data Set ◽  
X Ray ◽  
Cell Parameters ◽  
Peg 4000 ◽  
Drop Technique

The FNR-like domain of the Escherichia coli sulfite reductase flavoprotein subunit was crystallized using the hanging-drop technique, with PEG 4000 as precipitant. The crystals belong to space group P3112 or enantiomorph, with unit-cell parameters a = b = 171.0, c = 152.1 Å. A solvent content of 75% was determined by a calibrated tetrachloromethane/toluene gradient which corresponds to three monomers per asymmetric unit. A 3 Å resolution native data set was collected at beamline W32 of LURE, Orsay, France.

Crystallization and preliminary X-ray diffraction of Trypanosoma cruzi dUTPase

1999 ◽  
Vol 55 (2) ◽  
pp. 528-530 ◽  
Author(s):  
V. Bernier-Villamor ◽  
A. Camacho ◽  
D. González-Pacanowska ◽  
E. Cedergren-Zeppezauer ◽  
A. Antson ◽  
...  
Keyword(s):  
Trypanosoma Cruzi ◽  
Unit Cell ◽  
The Self ◽  
Asymmetric Unit ◽  
X Ray Diffraction ◽  
Solvent Content ◽  
X Ray ◽  
Cell Dimensions ◽  
Unit Cell Dimensions ◽  
Rotation Function

Crystals of Trypanosoma cruzi dUTPase have been grown. Two different morphologies are observed, depending on the molecular weight of the PEG used as precipitating agent in the mother liquor, both having a hexagonal unit cell with similar dimensions. Complete X-ray diffraction data have been collected to low resolution for one of the forms. The space group is P6322, with unit-cell dimensions a = 134.15, c = 147.05 Å. Peaks in the self-rotation function and the solvent content are consistent with two molecules of dUTPase per asymmetric unit.

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