scholarly journals New crystal forms of the integral membrane Escherichia coli quinol:fumarate reductase suggest that ligands control domain movement

2018 ◽  
Vol 202 (1) ◽  
pp. 100-104 ◽  
Author(s):  
C.A. Starbird ◽  
Thomas M. Tomasiak ◽  
Prashant K. Singh ◽  
Victoria Yankovskaya ◽  
Elena Maklashina ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Crystal Forms ◽  
Domain Movement

scholarly journals New crystal forms of the small subunit of ribonucleotide reductase from Escherichia coli

FEBS Letters ◽  
1989 ◽  
Vol 258 (2) ◽  
pp. 251-254 ◽  
Author(s):  
Par Nordlund ◽  
Ulla Uhlin ◽  
Christina Westergren ◽  
Thorleif Joelsen ◽  
Britt-Marie Sjöberg ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Ribonucleotide Reductase ◽  
Small Subunit ◽  
Crystal Forms

Metal-mediated crystallization of the xylose transporter XylE from Escherichia coli in three different crystal forms

2013 ◽  
Vol 184 (2) ◽  
pp. 375-378 ◽  
Author(s):  
Esben M. Quistgaard ◽  
Christian Löw ◽  
Per Moberg ◽  
Pär Nordlund
Keyword(s):  
Escherichia Coli ◽  
Crystal Forms ◽  
Xylose Transporter

Polymorphous crystallization and diffraction of threonine deaminase from Escherichia coli

1998 ◽  
Vol 54 (3) ◽  
pp. 467-469 ◽  
Author(s):  
D. Travis Gallagher ◽  
Edward Eisenstein ◽  
Kathryn E. Fisher ◽  
James Zondlo ◽  
Diana Chinchilla ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Diffraction Data ◽  
Crystal Form ◽  
Data Sets ◽  
Threonine Deaminase ◽  
Crystal Forms ◽  
Space Group ◽  
Regulatory Functions

The biosynthetic threonine deaminase from Escherichia coli, an allosteric tetramer with key regulatory functions, has been crystallized in several crystal forms. Two distinct forms, both belonging to either space group P3121 or P3221, with different sized asymmetric units that both contain a tetramer, grow under identical conditions. Diffraction data sets to 2.8 Å resolution (native) and 2.9 Å resolution (isomorphous uranyl derivative) have been collected from a third crystal form in space group I222.

scholarly journals Heat-labile enterotoxin of Escherichia coli. Characterization of different crystal forms.

1985 ◽  
Vol 260 (25) ◽  
pp. 13580-13584
Author(s):  
S E Pronk ◽  
H Hofstra ◽  
H Groendijk ◽  
J Kingma ◽  
M B Swarte ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Crystal Forms ◽  
Heat Labile

Purification and preliminary X-ray crystallographic studies of recombinant 7,8-diaminopelargonic acid synthase from Escherichia coli

1998 ◽  
Vol 54 (6) ◽  
pp. 1397-1398 ◽  
Author(s):  
Helena Käck ◽  
Katharine J. Gibson ◽  
Anthony A. Gatenby ◽  
Gunter Schneider ◽  
Ylva Lindqvist
Keyword(s):  
Escherichia Coli ◽  
Polyethylene Glycol ◽  
Pyridoxal Phosphate ◽  
Crystal Forms ◽  
X Ray ◽  
Space Groups ◽  
Cell Dimensions

Recombinant 7,8-diaminopelargonic acid synthase from Escherichia coli, a pyridoxal-phosphate-dependent aminotransferase, has been crystallized in space groups P21 and C2. Both crystal forms were obtained at pH 7.3 with 21% polyethylene glycol and 10% 2-propanol as precipitants. The cell dimensions were a = 130, b = 57.5, c = 117 Å, β = 110° for the C2 crystals, and a = 58.4, b = 55.6, c = 121 Å, β = 96.9° for the P21 crystals, which diffract to at least 2.6 and 2.0 Å resolution, respectively.

Two crystal forms of ModE, the molybdate-dependent transcriptional regulator from Escherichia coli

1999 ◽  
Vol 55 (2) ◽  
pp. 542-543 ◽  
Author(s):  
D. R. Hall ◽  
D. G. Gourley ◽  
E. M. H. Duke ◽  
G. A. Leonard ◽  
L. A. Anderson ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Structural Analysis ◽  
Biochemical Characterization ◽  
Regulatory Protein ◽  
Transcriptional Regulator ◽  
Structure Activity Relationship ◽  
Activity Relationship ◽  
Crystal Forms ◽  
Structure Activity ◽  
Medium Resolution

The molybdenum-responsive ModE regulatory protein from Escherichia coli has been purified and used in crystallization trials. Two crystal forms have been observed. Form I is tetragonal, P41212 (or enantiomorph), with a = b = 72.3, c = 246.2 Å and diffracts to medium resolution. Form II is orthorhombic, P21212, with a = 82.8, b = 127.9, c = 64.0 Å and diffraction has been observed beyond 2.8 Å resolution. Structural analysis, in combination with ongoing biochemical characterization, will assist the elucidation of the structure–activity relationship in regulating the uptake of molybdate in bacteria.

Expression, crystallization and preliminary X-ray analysis of ligand-free human glutathione S-transferase M2–2

1998 ◽  
Vol 54 (3) ◽  
pp. 458-460 ◽  
Author(s):  
Larysa N. Patskovska ◽  
Alexander A. Fedorov ◽  
Yury V. Patskovsky ◽  
Steven C. Almo ◽  
Irving Listowsky
Keyword(s):  
Escherichia Coli ◽  
Active Site ◽  
Asymmetric Unit ◽  
Glutathione S Transferase ◽  
Crystal Forms ◽  
Space Group ◽  
X Ray ◽  
Ligand Free ◽  
Catalytically Active ◽  
Insight Into

Human glutathione-S-transferase M2–2 (hGSTM2–2) was expressed in Escherichia coli and purified by GSH-affinity chromatography. The recombinant enzyme and the protein isolated from human tissue were indistinguishable based on physicochemical, enzymatic and immunological criteria. The catalytically active dimeric hGSTM2–2 was crystallized without GSH or other active-site ligands in two crystal forms. Diffraction from form A crystals extends to 2.5 Å and is consistent with the space group P21 (a = 53.9, b = 81.5, c = 55.6 Å, β = 109.26 Å) with two monomers in the asymmetric unit. Diffraction from form B crystals extends to 3 Å and is consistent with a space group P212121 (a = 57.2, b = 80.7, c = 225.9 Å) with two dimers in the asymmetric unit. This is the first report of ligand-free mu-class GST crystals, and a comparison with liganded complexes will provide insight into the structural consequences of substrate binding which are thought to be important for catalysis.

Disorder and twin refinement of RNA heptamer double helices

1999 ◽  
Vol 55 (8) ◽  
pp. 1405-1413 ◽  
Author(s):  
Uwe Mueller ◽  
Yves A. Muller ◽  
Regine Herbst-Irmer ◽  
Mathias Sprinzl ◽  
Udo Heinemann
Keyword(s):  
Escherichia Coli ◽  
Base Pair ◽  
Molecular Orientation ◽  
Molecular Models ◽  
Rna Structures ◽  
Base Pairs ◽  
Thermal Displacement ◽  
Crystal Forms ◽  
Space Group ◽  
Double Helices

An RNA helix with seven base pairs which was derived from the acceptor stem of Escherichia coli tRNAAla, rGGGGCUA·rUAGCUCC (ALAwt), as well as a variant, rGGGGCUA·rUAGCCCC (ALAC70), in which the single G·U wobble base pair of ALAwt was replaced by G·C, crystallize in space group C2. Both non-isomorphic crystal forms display a complex packing pattern, which can be described alternatively as disorder or pseudo-merohedral twinning. The structure of ALAwt was determined by SIRAS phasing using an isomorphous iodine derivative, rGGGGCi5UA·rUAGCUCC (ALAI). All three RNA structures were subsequently subjected to twin refinement in space group P1, using anisotropic thermal displacement parameters at resolutions of 1.16, 1.23 and 1.4 Å for ALAwt, ALAI and ALAC70, respectively. Alternatively, the structure of ALAwt was refined in space group C2 assuming twofold disorder of the molecular orientation. The refined structures are of reasonable quality according to all available indicators. There are no systematic differences between the molecular models resulting from twin refinement and disorder refinement.

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