title: Crystallization and preliminary crystallographic analysis of recombinant human calcyphosine.
abstract: Human calcyphosine was cloned into the pET-28a vector and highly expressed in Escherichia coli BL21 (DE3) cells. The protein was purified and crystallized. The crystal diffracted to 2.8 A and belonged to space group P2(1)2(1)2, with the unit cell parameters a=70.39 A, b=132.02 A, c=46.20 A.
authors.affiliation: Laboratory of Structural Biology, Tsinghua University, Beijing 100084, China.
authors.forename: Hui
authors.initials: H
authors.lastname: Dong
authors.forename: Zhiyong
authors.initials: Z
authors.lastname: Lou
authors.forename: Xiaoling
authors.initials: X
authors.lastname: Xu
authors.forename: Dan
authors.initials: D
authors.lastname: Su
authors.forename: Xiaohong
authors.initials: X
authors.lastname: Zhou
authors.forename: Xin
authors.initials: X
authors.lastname: Li
authors.forename: Mark
authors.initials: M
authors.lastname: Bartlam
mesh_terms: D002135:Calcium-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics; D006801:Humans; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification
chemical_list: C059605:CAPS protein, human; D002135:Calcium-Binding Proteins; D011994:Recombinant Proteins