Crystallization and preliminary X‐ray diffraction studies of the calcium‐binding protein CalD from Streptomyces coelicolor
Calcium ions play an important regulatory role in eukaryotes. However, the regulatory roles of Ca2+ in prokaryotes are poorly understood. CalD, an 18 kDa calcium‐binding protein from the model actinomycete Streptomyces coelicolor A3(2), was purified and crystallized for structure determination by X‐ray crystallography. Crystals of CalD that were suitable for X‐ray diffraction were obtained using the hanging‐drop vapour‐diffusion method and diffraction data were collected in‐house to 1.56 Å resolution. The crystals belonged to space group P212121, with unit‐cell parameters a = 32.9, b = 51.0, c = 87.0 Å, α = β = γ = 90.0°. There is one protein molecule per asymmetric unit.
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