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 |
Fingerprint
Keywords
- Crystallization
- Phospholipid transfer protein
- Possible amylase/protease inhibitor
- Preliminary X-ray analysis
- Rice seeds
ASJC Scopus subject areas
- Virology
Cite this
Crystallization and preliminary X-ray crystallographic analysis of probable amylase/protease inhibitor-B from rice seeds. / Hwang, Kwang Yeon; Kim, Kyeong Kyu; Min, Kyeongsik; Eom, Soo Hyun; Yu, Yeon Gyu; Kim, Sangsoo; Sweet, Robert M.; Suh, Se Won.
In: Journal of Molecular Biology, Vol. 229, No. 1, 01.12.1993, p. 255-257.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Crystallization and preliminary X-ray crystallographic analysis of probable amylase/protease inhibitor-B from rice seeds
AU - Hwang, Kwang Yeon
AU - Kim, Kyeong Kyu
AU - Min, Kyeongsik
AU - Eom, Soo Hyun
AU - Yu, Yeon Gyu
AU - Kim, Sangsoo
AU - Sweet, Robert M.
AU - Suh, Se Won
PY - 1993/12/1
Y1 - 1993/12/1
N2 - 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.
AB - 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.
KW - Crystallization
KW - Phospholipid transfer protein
KW - Possible amylase/protease inhibitor
KW - Preliminary X-ray analysis
KW - Rice seeds
UR - http://www.scopus.com/inward/record.url?scp=0027508876&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0027508876&partnerID=8YFLogxK
M3 - Article
C2 - 8421310
AN - SCOPUS:0027508876
VL - 229
SP - 255
EP - 257
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
SN - 0022-2836
IS - 1
ER -