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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.