Crystallisation and preliminary X-ray diffraction studies of cyclophilin-tetrapeptide and cyclophilin-cyclosporin complexes
| Autor: | Johan N. Jansonius, Gaston Pfluegl, Joerg Kallen, Malcolm D. Walkinshaw, Vincent Mikol, Mauro G. M. Zurini |
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| Rok vydání: | 1990 |
| Předmět: |
Protein Conformation
Stereochemistry Molecular Sequence Data Biophysics Cyclosporins Crystal structure Biochemistry Tetragonal crystal system Protein structure X-Ray Diffraction Coumarins Structural Biology Genetics Amino Acid Sequence Molecular Biology Peptide sequence Cyclophilin Amino Acid Isomerases Cyclosporin Peptidylprolyl isomerase Linear dichroism Tetrapeptide Chemistry Protein crystallisation Cell Biology Peptidylprolyl Isomerase Crystallography X-ray crystallography Cis-trans isomerase Carrier Proteins Crystallization Oligopeptides Protein Binding |
| Zdroj: | FEBS Letters. 276:63-66 |
| ISSN: | 0014-5793 |
| Popis: | 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-amidomethyl-coumarin (I) which crystallises in space group P2(1)2(1)2(1) with a = 108.2, b = 123.0, c = 35.8 A, 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 A. |
| Databáze: | OpenAIRE |
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