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

FEBS Letters

Mikol, Vincent²  Pfluegl, Gaston¹  Kallen, Joerg²  Jansonius, Johan N.¹  Walkinshaw, Malcolm D.²  Zurini, Mauro² 

[1] Biocentre, University Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland;Preclinical Research, Sandoz Pharma AG, CH-4002 Basel, Switzerland

关键词: Cyclophilin;    Cyclosporin;    Protein crystallisation;    Cis-trans isomerase;    Linear dichroism;   

DOI  :  10.1016/0014-5793(90)80507-F

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 P2₁2₁2₁ with a = 108.2, b = 123.0, c = 35.8 Å, and cyclophilin with cyclosporin (II) which crystallises as tetragonal plates in space group P4₁2₁2 or P4₃2₁2 with a = b = 94.98, c = 278.55 Å.

【 授权许可】

Unknown