title: Crystallization and preliminary X-ray diffraction studies of the calcium-binding protein CalD from Streptomyces coelicolor.
abstract: Calcium ions play an important regulatory role in eukaryotes. However, the regulatory roles of Ca(2+) 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 A resolution. The crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 32.9, b = 51.0, c = 87.0 A, alpha = beta = gamma = 90.0 degrees . There is one protein molecule per asymmetric unit.
authors.affiliation: Laboratory of Structural Biology, Tsinghua University, Beijing 100084, People's Republic of China.
authors.forename: Xiaoyan
authors.initials: X
authors.lastname: Zhao
authors.forename: Shenglan
authors.initials: S
authors.lastname: Wang
authors.forename: Hai
authors.initials: H
authors.lastname: Pang
authors.forename: Keqian
authors.initials: K
authors.lastname: Yang
authors.forename: Mark
authors.initials: M
authors.lastname: Bartlam