D-Serine dehydratase from Escherichia coli is a member of the β-family (fold-type II) of the pyridoxal 5'-phosphate-dependent enzymes, catalyzing the conversion of D-serine to pyruvate and ammonia. The crystal structure of monomeric D-serine dehydratase has been solved to 1.97Å-resolution for an orthorhombic data set by molecular replacement. In addition, the structure was refined in a monoclinic data set to 1.55Å resolution. The structure of DSD reveals a larger pyridoxal 5'-phosphate-binding domain and a smaller domain. The active site of DSD is very similar to those of the other members of the β-family. Lys118 forms the Schiff base to PLP, the cofactor phosphate group is liganded to a tetraglycine cluster Gly279-Gly283, and the 3-hydroxyl group of PLP is liganded to Asn170 and N1 to Thr424, respectively. In the closed conformation the movement of the small domain blocks the entrance to active site of DSD. The domain movement plays an important role in the formation of the substrate recognition site and the catalysis of the enzyme. Modeling of D-serine into the active site of DSD suggests that the hydroxyl group of D-serine is coordinated to the carboxyl group of Asp238. The carboxyl oxygen of D-serine is coordinated to the hydroxyl group of Ser167 and the amide group of Leu171 (O1), whereas the O2 of the carboxyl group of D-serine is hydrogen-bonded to the hydroxyl group of Ser167 and the amide group of Thr168. A catalytic mechanism very similar to that proposed for L-serine dehydratase is discussed.

Achieving optimal design and precise control of the internal structure of laser-target materials are the primary objectives in various laser physics experiments, particularly in generating high flux photon and neutron beams. The study of low-density materials poses considerable challenges for X-ray analysis due to their high transparency and minimal contrast. In this study, to obtain clear visualization of foams with sparse structures, we used phase-contrast X-ray tomography, utilizing a high-quality monochromatic X-ray beam from the synchrotron radiation source PETRA-III at DESY. Employing phase-contrast algorithms, the 3D structure of a foam-suspended glass microsphere inside the plastic cylinder was reconstructed with a level of image quality sufficient to visualize uniformity, displacement, and surface roughness on both sides of the microsphere. The primary focus of this investigation was a CH plastic capillary including 10 mg/cc CHO foam with a glass microsphere positioned at the center. The results of this study demonstrate that phase-contrast X-ray tomography with coherent synchrotron radiation is an effective and valuable technique for the development of new laser targets containing structured low-density materials.