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. The crystals presented symmetry compatible with the space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 58.71, c = 93.75 A, and diffracted to 1.83 A resolution at the synchrotron source.
Krauchenco
S
S
Laboratório Nacional de Luz Síncrotron, Campinas, SP, Brazil.
Silva
J A
JA
Nagem
R A
RA
Brandão Neto
J R
JR
Forrer
V P
VP
Carmona E Ferreira
R
R
Macedo
M L
ML
Novello
J C
JC
Marangoni
S
S
Polikarpov
I
I
D003460:Crystallization; D018360:Crystallography, X-Ray; D007887:Fabaceae / Q000737:chemistry*; D008565:Membrane Proteins; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry*; D011487:Protein Conformation; D029701:Saccharomyces cerevisiae Proteins; D012639:Seeds / Q000737:chemistry; D020539:Sequence Analysis, Protein; D017386:Sequence Homology, Amino Acid; D014361:Trypsin Inhibitors / Q000737:chemistry* / Q000302:isolation & purification
C438144:ASI1 protein, S cerevisiae; D008565:Membrane Proteins; D010940:Plant Proteins; D029701:Saccharomyces cerevisiae Proteins; D014361:Trypsin Inhibitors