Abstract
Large crystals of probable amylase/protease inhibitor-B have been grown at room temperature from ammonium sulfate solution. The crystals grow within five days to dimensions of 0.6 mm x 0.6 mm x 0.6 mm. They diffract to at least 1.7 Å upon exposure to synchrotron X-rays. The crystals belong to the space group P41212 (or P43212) with unit cell dimensions of a = 38.02 Å and c = 98.98 Å. The presence of one molecule per asymmetric unit gives the unit cell volume per protein mass (Vm) of 1.99 Å3/Da and the solvent fraction of 38.2% by volume. X-ray data have been collected to 2.0 Å Bragg spacing from native crystals.
| Original language | English |
|---|---|
| Pages (from-to) | 255-257 |
| Number of pages | 3 |
| Journal | Journal of Molecular Biology |
| Volume | 229 |
| Issue number | 1 |
| Publication status | Published - 1993 Dec 1 |
| Externally published | Yes |
Keywords
- Crystallization
- Phospholipid transfer protein
- Possible amylase/protease inhibitor
- Preliminary X-ray analysis
- Rice seeds
ASJC Scopus subject areas
- Virology
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Hwang, K. Y., Kim, K. K., Min, K., Eom, S. H., Yu, Y. G., Kim, S., Sweet, R. M., & Suh, S. W. (1993). Crystallization and preliminary X-ray crystallographic analysis of probable amylase/protease inhibitor-B from rice seeds. Journal of Molecular Biology, 229(1), 255-257.