Crystallization and preliminary X-ray analysis of the periplasmic receptor (PotF) of the putrescine transport system in Escherichia coli

1998 ◽  
Vol 54 (1) ◽  
pp. 132-134 ◽  
Author(s):  
Dmitry G. Vassylyev ◽  
Tatsuki Kashiwagi ◽  
Hideyuki Tomitori ◽  
Keiko Kashiwagi ◽  
Kazuei Igarashi ◽  
...  
Keyword(s):  
Transport System ◽  
Heavy Atom ◽  
Hanging Drop ◽  
Data Set ◽  
X Ray ◽  
E Coli ◽  
Diffusion Technique ◽  
Cell Dimensions ◽  
The Difference ◽  
Unit Cell Dimensions

The primary receptor (PotF) of the putrescine transport system in E. coli has been crystallized by the hanging-drop vapor-diffusion technique. The crystals belong to the space group P21212 with unit-cell dimensions a = 269.4, b = 82.33 and c = 93.74 Å. The crystals diffract beyond 2.2 Å with a rotating-anode X-ray source. A complete data set from the native crystals has been collected and processed at 2.3 Å resolution. Two heavy-atom derivatives have been prepared from the same Pt compound at 293 and 277 K. The difference Patterson maps revealed completely different major heavy-atom sites between these two derivatives.

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 X-ray analysis of polyamine oxidase from Zea mays L.

1998 ◽  
Vol 54 (6) ◽  
pp. 1429-1431 ◽  
Author(s):  
Claudia Binda ◽  
Alessandro Coda ◽  
Riccardo Angelini ◽  
Rodolfo Federico ◽  
Paolo Ascenzi ◽  
...  
Keyword(s):  
Zea Mays L ◽  
Polyamine Oxidase ◽  
Amine Oxidases ◽  
Hanging Drop ◽  
Data Set ◽  
X Ray ◽  
Diffusion Technique ◽  
The Family ◽  
Cell Dimensions ◽  
Secondary Amino

Polyamine oxidase catalyses the oxidation of the secondary amino group of spermine, spermidine and their acetyl derivatives. The enzyme plays an important role in the regulation of polyamine intracellular concentration and is a member of the family of flavin-containing amine oxidases. Crystals of maize polyamine oxidase have been grown by the hanging-drop vapour-diffusion technique. The crystals are in hexagonal space group P6122 (or P6522) with cell dimensions a = b = 184.6, c = 280.9 Å. A native data set has been collected to 2.7 Å resolution at a synchrotron radiation source.

Preliminary X-ray analysis of a new crystal form of the vanadium-dependent bromoperoxidase from Corallina officinalis

1998 ◽  
Vol 54 (3) ◽  
pp. 454-457 ◽  
Author(s):  
Amanda A. Brindley ◽  
Andrew R. Dalby ◽  
Michail N. Isupov ◽  
Jennifer A. Littlechild
Keyword(s):  
Heavy Atom ◽  
Crystal Form ◽  
Dihydrogen Phosphate ◽  
Data Set ◽  
X Ray ◽  
Heavy Atoms ◽  
Corallina Officinalis ◽  
Cell Dimensions ◽  
Unit Cell Dimensions ◽  
Rotation Function

A new crystal form of the vanadium-dependent bromoperoxidase from Corallina officinalis has been obtained. The crystals exhibit a `teardrop' morphology and are grown from 2 M ammonium dihydrogen phosphate pH 5 and diffract to beyond 1.7 Å resolution. They are in tetragonal space group P4222 with unit-cell dimensions of a = b = 201.9, c = 178.19 Å, α = β = γ = 90°. A 2.3 Å resolution native data set has been collected at the Hamburg Synchrotron. A mercury derivative data set has also been collected, and the heavy-atom positions have been determined. The self-rotation function and the positions of the heavy atoms are consistent with the molecule being a dodecamer with local 23 symmetry.

Crystallization and preliminary X-ray diffraction studies of E. coli porphobilinogen synthase and its heavy-atom derivatives

1998 ◽  
Vol 54 (3) ◽  
pp. 438-440 ◽  
Author(s):  
L. Shimoni-Livny ◽  
H. L. Carrell ◽  
T. Wagner ◽  
A. Kaufman Katz ◽  
C. Afshar ◽  
...  
Keyword(s):  
Active Sites ◽  
Aminolevulinic Acid ◽  
Heavy Atom ◽  
Unit Cell ◽  
X Ray Diffraction ◽  
X Ray ◽  
E Coli ◽  
Cell Dimensions ◽  
Porphobilinogen Synthase ◽  
Unit Cell Dimensions

Porphobilinogen synthase (PBGS) catalyzes the condensation of two identical substrate molecules, 5-aminolevulinic acid (ALA), in an asymmetric manner to form porphobilinogen. E. coli PBGS is an homooctameric enzyme. The number of active sites is not clear, but each subunit binds one ZnII ion and one MgII ion. Diffraction-quality crystals of native E. coli PBGS have been obtained, and unit-cell dimensions (a = 130.8, c = 144.0 Å) are reported. These crystals diffract to about 3.0 Å resolution.

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 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 of L-aspartate oxidase, the first enzyme in the bacterial de novo biosynthesis of NAD

1999 ◽  
Vol 55 (2) ◽  
pp. 549-551 ◽  
Author(s):  
Luca Bacchella ◽  
Claudio Lina ◽  
Flavia Todone ◽  
Armando Negri ◽  
Gabriella Tedeschi ◽  
...  
Keyword(s):  
De Novo ◽  
Asymmetric Unit ◽  
Hanging Drop ◽  
Unit Cell Parameters ◽  
Data Set ◽  
X Ray ◽  
Cell Parameters ◽  
De Novo Biosynthesis ◽  
Diffusion Technique ◽  
Peg 4000

The flavoenzyme L-aspartate oxidase from Escherichia coli was crystallized using the hanging-drop vapour-diffusion technique with PEG 4000 as precipitant. The crystals belong to space group P3121 (or P3221) with unit-cell parameters a = b = 84.9, c = 159.9 Å. A solvent content of 42% corresponds to a monomer (60 kDa) in the asymmetric unit. A complete 2.8 Å resolution data set was collected using a rotating-anode X-ray generator.

Expression, purification, crystallization and preliminary X-ray analysis of Escherichia coli argininosuccinate synthetase

1999 ◽  
Vol 55 (12) ◽  
pp. 2028-2030 ◽  
Author(s):  
Chris Lemke ◽  
Melissa Yeung ◽  
P. Lynne Howell
Keyword(s):  
Escherichia Coli ◽  
National Laboratory ◽  
Brookhaven National Laboratory ◽  
Argininosuccinate Synthetase ◽  
Affinity Tag ◽  
X Ray ◽  
Diffusion Technique ◽  
Cell Dimensions ◽  
Synchrotron Light ◽  
Unit Cell Dimensions

A recombinant form of Escherichia coli argininosuccinate synthetase with a C-terminal polyhistidine affinity tag has been expressed, purified and subsequently crystallized using the hanging-drop vapour-diffusion technique. The crystals grow as large rectangular chunks with unit-cell dimensions a = 79.70, b = 105.84, c = 127.33 Å, α = β = γ = 90°. The crystals exhibit the symmetry of space group I222 and diffract to a minimum d-spacing of 1.6 Å at station X8C of the National Synchrotron Light Source, Brookhaven National Laboratory. On the basis of density calculations, one monomer of this homotetrameric protein is predicted per asymmetric unit (Matthews coefficient Vm = 2.69 Å3 Da−1).

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.

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