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. 2005 Sep 1;61(Pt 9):841-3.
doi: 10.1107/S1744309105024462. Epub 2005 Aug 31.

Crystallization and preliminary X-ray diffraction analysis of a new chitin-binding protein from Parkia platycephala seeds

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Crystallization and preliminary X-ray diffraction analysis of a new chitin-binding protein from Parkia platycephala seeds

Benildo S Cavada et al. Acta Crystallogr Sect F Struct Biol Cryst Commun. .

Abstract

A chitin-binding protein named PPL-2 was purified from Parkia platycephala seeds and crystallized. Crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 55.19, b = 59.95, c = 76.60 A, and grew over several days at 293 K using the hanging-drop method. Using synchrotron radiation, a complete structural data set was collected to 1.73 A resolution. The preliminary crystal structure of PPL-2, determined by molecular replacement, presents a correlation coefficient of 0.558 and an R factor of 0.439. Crystallographic refinement is in progress.

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Figures

Figure 1
Figure 1
PPL-2 crystals. (a) Crystal cluster from PPL-2 seeding. (b) Crystals of PPL-2 diffracted to 1.73 Å.
Figure 2
Figure 2
Multiple alignment of the N-terminal sequence of PPL-2 with those of plant chitinases. GmCHI, acidic chitinase from G. max; ZmCHI, acidic chitinase from Z. mays; Hevamina, chitinase/lysozyme from H. brasiliensis; VvCHI, precursor of acidic chitinase from Vitis vinifera; AtCHI, acidic endochitinase from A. thaliana; VuCHI, basic endochitinase type III from Vigna unguiculata; PaCHI, chitinase-B from Phytolacca americana; NtCHI, basic endochitinase type III from N. tabacum.

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