Crystallization and preliminary X-ray diffraction analysis of a novel trypsin inhibitor from seeds of Copaifera langsdorffii

A novel trypsin inhibitor isolated from seeds of Copaifera langsdorffii was purified to homogeneity and crystallized. Crystals suitable for X‐­ray analysis were grown using the hanging‐drop vapour‐diffusion method at 291 K in sodium acetate buffer at pH values near 4.3 using PEG 4000 as precipitant....

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Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2001-09, Vol.57 (9), p.1316-1318
Main Authors: Krauchenco, S., Silva, J. A., Nagem, R. A. P., Brandão Neto, J. R., Forrer, V. P., Carmona e Ferreira, R., Macedo, M. L. R., Novello, J. C., Marangoni, S., Polikarpov, I.
Format: Article
Language:English
Subjects:
Copaifera langsdorffii
Crystallization
Crystallography, X-Ray
Fabaceae - chemistry
Membrane Proteins
Molecular Sequence Data
Plant Proteins - chemistry
Protein Conformation
Saccharomyces cerevisiae Proteins
Seeds - chemistry
Sequence Analysis, Protein
Sequence Homology, Amino Acid
trypsin inhibitor
Trypsin Inhibitors - chemistry
Trypsin Inhibitors - isolation & purification
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Summary:A novel trypsin inhibitor isolated from seeds of Copaifera langsdorffii was purified to homogeneity and crystallized. Crystals suitable for X‐­ray analysis were grown using the hanging‐drop vapour‐diffusion method at 291 K in sodium acetate buffer at pH values near 4.3 using PEG 4000 as precipitant. The crystals presented symmetry compatible with the space group P41212 or P43212, with unit‐cell parameters a = b = 58.71, c = 93.75 Å, and diffracted to 1.83 Å resolution at the synchrotron source.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444901011131