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

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.

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

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)38763-x ◽

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

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

Acta Crystallographica Section D Biological Crystallography ◽

10.1107/s0907444998001954 ◽

1998 ◽

Vol 54 (6) ◽

pp. 1397-1398 ◽

Cited By ~ 7

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.

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

Acta Crystallographica Section D Biological Crystallography ◽

10.1107/s0907444998011354 ◽

1999 ◽

Vol 55 (2) ◽

pp. 542-543 ◽

Cited By ~ 5

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.

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An evolved xylose transporter from Zymomonas mobilis enhances sugar transport in Escherichia coli

Microbial Cell Factories ◽

10.1186/1475-2859-8-66 ◽

2009 ◽

Vol 8 (1) ◽

pp. 66 ◽

Cited By ~ 31

Author(s):

Chuan Ren ◽

Tingjian Chen ◽

Jingqing Zhang ◽

Ling Liang ◽

Zhanglin Lin

Keyword(s):

Escherichia Coli ◽

Zymomonas Mobilis ◽

Sugar Transport ◽

Xylose Transporter

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

Acta Crystallographica Section D Biological Crystallography ◽

10.1107/s0907444997011190 ◽

1998 ◽

Vol 54 (3) ◽

pp. 458-460 ◽

Cited By ~ 3

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.

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