Crystallization and preliminary X-ray characterization of the acylphosphatase-like domain from the Escherichia coli hydrogenase maturation factor HypF

The prokaryotic hydrogenase maturation factor protein HypF (82 kDa) contains a 10 kDa domain displaying structural homology to prokaryotic and eukaryotic acylphosphatases. Two different crystal forms of the HypF N-terminal domain have been characterized.

Structural plasticity in the eight-helix fold of a trematode haemoglobin

Analysis of the crystal structure of a trematode haemoglobin displaying very high O₂ affinity shows that crystal contacts in two different crystal forms markedly affect the haem-cavity stereochemistry and haem Fe coordination state.

Crystallization and preliminary X-ray diffraction analysis of brefeldin A-ADP ribosylated substrate (BARS)

A truncated form of brefeldin A-ADP ribosylated substrate (residues 1–350), a protein involved in Golgi membrane fission, has been expressed, purified and crystallized. SeMet-substituted crystals were also prepared, aiming at the three-dimensional structure solution via MAD methods.

Crystallization and preliminary crystallographic characterization of the extracellular Ig-like domain of human natural killer cell activating receptor NKp44

NKp44, a natural killer cell activating receptor, is composed of an extracellular region (168 amino acids), a membrane-spanning segment (25 amino acids) and a cytoplasmic domain (63 amino acids). The extracellular region Ig-like domain, held to be involved in target-cell recognition/binding, has been crystallized in a form suitable for structural investigation.

Human neuroglobin: crystals and preliminary X-ray diffraction analysis

Human neuroglobin (151 amino acids), a haemoglobin involved in the neuronal response to hypoxia or ischaemia, has been expressed, purified and crystallized as a Cys-free mutant protein, with a view to three-dimensional structure determination.