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

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.

doi:10.1107/S0907444901011131

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

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Figure 1
SDS–PAGE using a 16.5% tricine gel. Lane 1 shows the molecular-weight standards: phosphorylase (MW = 94 kDa), albumin (MW = 66 kDa), egg albumin (MW = 43 kDa), carbonic anhydrase (MW = 30 kDa), pancreas trypsin inhibitor (MW = 20 kDa) and cytochrome (MW = 12 kDa). Lane 2 shows the inhibitor extracted from C. langsdorffii seeds and reduced with 0.1 M DTT. Lanes 3 and 4 show the two non-covalently bound parts of the molecule separated with 0.1 M DTT and purified by HPLC using a reverse-phase column. Lane 5 shows the inhibitor from dissolved crystal.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 57| Part 9| August 2001| Pages 1316-1318

doi:10.1107/S0907444901011131

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