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A soluble mutant (I6T/V47M/T69M) of the Rv2002 gene product (FabG3) of M. tuberculosis was crystallized. The X-ray diffraction quality of the crystal improved significantly after annealing/dehydration, enabling data collection to 1.8 Å resolution.

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β-Xylosidase from the thermophilic anaerobe T. saccharolyticum has been crystallized at 296 K using the hanging-drop vapour-diffusion method. The crystal diffracts to 2.4 Å resolution with synchrotron X-rays.

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Aspartate 1-decarboxylase (PanD) from H. pylori has been overexpressed and crystallized (space group I422; unit-cell parameters a = b = 81.83, c = 93.78 Å). Diffraction data have been collected to 1.55 Å using synchrotron X-rays.

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Peptide deformylase from P. aeruginosa has been crystallized (P212121; a = 68.75, b = 74.46, c = 77.18 Å). Diffraction data have been collected to 1.85 Å using synchrotron X-rays.

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Acetohydroxy acid isomeroreductase from P. aeruginosa was crystallized. X-ray data have been collected to 2.0 Å resolution using synchrotron radiation (P213, a = b = c = 184.38 Å).
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