title: Purification, characterization and crystallization in two crystal forms of bovine cyclophilin 40.
abstract: The purification and crystallization of two different crystal forms of the two-domain protein bovine cyclophilin 40 is reported. Tetragonal crystals grown in methyl pentanediol belong to space group P4222 with unit-cell parameters a = 94.5, c = 118.3 A. Long thin needles grown from PEG belong to space group C2 with unit-cell parameters a = 125.71, b = 47.3, c = 74.6 A, beta = 93.90 degrees. The N-terminal 170 amino acids have significant homology with the well characterized human cyclophilin A. The C-terminal domain is largely made up of three copies of the tetratricopeptide repeat motif thought to be involved in mediating protein-protein interactions. Cyclophilins are frequently found as domains in larger multidomain proteins. To date, only X-ray structures of single-domain cyclophilins have been reported, and this work provides the first example of the purification and crystallization of a larger protein containing a cyclophilin domain.
authors.affiliation: Structural Biochemistry Group, Institute of Cell and Molecular Biology, The University of Edinburgh, Michael Swann Building, King's Buildings, Mayfield Road, Edinburgh EH9 3JR, Scotland.
authors.forename: J
authors.initials: J
authors.lastname: Dornan
authors.forename: P
authors.initials: P
authors.lastname: Taylor
authors.forename: A
authors.initials: A
authors.lastname: Carrello
authors.forename: R F
authors.initials: RF
authors.lastname: Minchin
authors.forename: T
authors.initials: T
authors.lastname: Ratajczak
authors.forename: M D
authors.initials: MD
authors.lastname: Walkinshaw
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D017173:Caenorhabditis elegans; D002352:Carrier Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D002417:Cattle; D016384:Consensus Sequence; D003460:Crystallization; D000081406:Peptidyl-Prolyl Isomerase F; D021983:Cyclophilins; D005982:Glutathione Transferase / Q000096:biosynthesis / Q000235:genetics; D006801:Humans; D008969:Molecular Sequence Data; D019696:Peptidylprolyl Isomerase / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D017386:Sequence Homology, Amino Acid
chemical_list: D002352:Carrier Proteins; D000081406:Peptidyl-Prolyl Isomerase F; D011993:Recombinant Fusion Proteins; D005982:Glutathione Transferase; D021983:Cyclophilins; D019696:Peptidylprolyl Isomerase