Crystallisation and preliminary X‐ray diffraction studies of cyclophilin‐tetrapeptide and cyclophilin‐cyclosporin complexes | Zendy

Zurini Mauro | Zendy; Kallen Joerg | Zendy; Mikol Vincent | Zendy; Pfluegl Gaston | Zendy; Jansonius Johan N. | Zendy; Walkinshaw Malcolm D. | Zendy

Premium

Crystallisation and preliminary X‐ray diffraction studies of cyclophilin‐tetrapeptide and cyclophilin‐cyclosporin complexes

Author(s) -

Zurini Mauro,

Kallen Joerg,

Mikol Vincent,

Pfluegl Gaston,

Jansonius Johan N.,

Walkinshaw Malcolm D.

Publication year - 1990

Publication title -

febs letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.593

H-Index - 257

eISSN - 1873-3468

pISSN - 0014-5793

DOI - 10.1016/0014-5793(90)80507-f

Subject(s) - cyclophilin , cyclophilin a , crystallography , tetragonal crystal system , x ray crystallography , tetrapeptide , chemistry , crystallization , x ray , stereochemistry , crystal structure , biology , diffraction , microbiology and biotechnology , biochemistry , peptide , physics , organic chemistry , gene , optics , quantum mechanics

Recombinant human cyclophilin has been co‐crystallised with a number of peptides to give crystals suitable for X‐ray analysis. The crystal complexes for which heavy‐atom derivatives have been prepared and X‐ray data collected are: cyclophilin with N ‐acetyl‐Ala‐Ala‐Pro‐Ala‐amidomethylcoumarin (I) which crystallises in space group P2 1 2 1 2 1 with a = 108.2, b = 123.0, c = 35.8 Å, and cyclophilin with cyclosporin (II) which crystallises as tetragonal plates in space group P4 1 2 1 2 or P4 3 2 1 2 with a = b = 94.98, c = 278.55 Å.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research