The recombinant BPTI/Kunitz-type inhibitor rShPI-1A from the Caribbean sea anemone S. helianthus has been crystallized and its structure has been refined to 2.5 Å resolution and compared with known X-ray structures of BPTI-like Kunitz-type inhibitors.
Binding of cisplatin to His15 in hen egg-white lysozyme in aqueous media is observed after prolonged chemical exposure for 15 months, in contrast to the lack of binding that was observed after 4 d in a previous study. Binding of carboplatin is seen in greater detail in the case of room-temperature data collection compared with cryo data collection.
This article describes the crystallization and preliminary crystallographic analysis of a protein construct (hCBS516–525) that contains the full-length cystathionine β-synthase from Homo sapiens (hCBS) and just lacks amino-acid residues 516–525.
This manuscript describes the crystallization of the full-length enzyme cystathionine β-synthase (CBS) from Apis mellifera, which maintains 46% sequence identity with the human homolog. Mutations in CBS cause hereditary homocystinuria in humans.
The ETS domain of human Ergp55 was purified and crystallized in native, complexes with E74, and cfos promoter DNA sequences. The X-ray intensity data set was collected on ETS–cfos promoter DNA complex crystal at 3.1 Å resolution to analyze the structure by molecular replacement technique.
ID2 is an inhibitor of DNA binding that is known to be highly unstable. This study describes the cloning, expression and purification of ID2 for crystallization, culminating in the collection of diffraction data.
The myelin protein P2 is a peripheral membrane protein functional in lipid bilayer binding and stacking. In order to study the fine details of P2 structure and function, 14 point mutants of human P2 were generated and crystallized; a total of eight different crystal forms were obtained, some of which diffracted to atomic resolution.
Crystallization and diffraction analysis of a Ca2+-dependent PI-PLC from Streptomyces is reported. Optimization of crystals was completed using a drop-pinning technique and heavy-atom soaks to achieve high-quality diffraction to 1.23 Å.
A complex comprising the LIM domains of the LIM-homeodomain protein Isl1 tethered to a peptide region of Ldb1 has been engineered, purified and crystallized. Crystals of this intramolecular complex diffracted to 3.10 Å resolution.