Crystallization and preliminary X-ray analysis of the CRP-cAMP-DNA (full length) complex

The Escherichia coli cyclic AMP receptor protein (CRP) crystals were obtained and diffracted at a 2.9 Å resolution, which belonged to the space group P3₁21, with unit-cell parameters a = b = 76.03, c = 144.00 Å. The asymmetric unit was found to contain one protein molecule and a half 38 bp full-length double-stranded DNA fragment with a Matthews coefficient of 2.62 Å³ Da^-1 and a solvent content of 53.14%.

Crystallization and preliminary X-ray diffraction analysis of a thermostable GDSL-family esterase, EstL5, from Geobacillus thermodenitrificans T2

As a thermostable esterase with cold adaptation, EstL5 might be of significant industrial interest and value in scientific research. In order to provide new insights into the structure-function relationship of EstL5 and to help better understand the biochemical data, a project to determine the three-dimensional structure of this enzyme was initiated.