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Crystallization and preliminary X-ray crystallographic analysis of probable amylase/protease inhibitor-B from rice seeds.
J Mol Biol. 1993 Jan 05; 229(1):255-7.JM

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 A upon exposure to synchrotron X-rays. The crystals belong to the space group P4(1)2(1)2 (or P4(3)2(1)2) with unit cell dimensions of a = 38.02 A and c = 98.98 A. The presence of one molecule per asymmetric unit gives the unit cell volume per protein mass (Vm) of 1.99 A3/Da and the solvent fraction of 38.2% by volume. X-ray data have been collected to 2.0 A Bragg spacing from native crystals.

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Authors+Show Affiliations

Hwang KY
Department of Chemistry, College of Natural Sciences Seoul National University, Korea.
Kim KK
No affiliation info available
Min K
No affiliation info available
Eom SH
No affiliation info available
Yu YG
No affiliation info available
Kim S
No affiliation info available
Sweet RM
No affiliation info available
Suh SW
No affiliation info available

MeSH

CrystallizationOryzaPlant ProteinsProtease InhibitorsX-Ray Diffractionalpha-Amylases

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

Language

eng

PubMed ID

8421310

Citation

Hwang, K Y., et al. "Crystallization and Preliminary X-ray Crystallographic Analysis of Probable Amylase/protease inhibitor-B From Rice Seeds." Journal of Molecular Biology, vol. 229, no. 1, 1993, pp. 255-7.
Hwang KY, Kim KK, Min K, et al. Crystallization and preliminary X-ray crystallographic analysis of probable amylase/protease inhibitor-B from rice seeds. J Mol Biol. 1993;229(1):255-7.
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), 255-7.
Hwang KY, et al. Crystallization and Preliminary X-ray Crystallographic Analysis of Probable Amylase/protease inhibitor-B From Rice Seeds. J Mol Biol. 1993 Jan 5;229(1):255-7. PubMed PMID: 8421310.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and preliminary X-ray crystallographic analysis of probable amylase/protease inhibitor-B from rice seeds. AU - Hwang,K Y, AU - Kim,K K, AU - Min,K, AU - Eom,S H, AU - Yu,Y G, AU - Kim,S, AU - Sweet,R M, AU - Suh,S W, PY - 1993/1/5/pubmed PY - 1993/1/5/medline PY - 1993/1/5/entrez SP - 255 EP - 7 JF - Journal of molecular biology JO - J Mol Biol VL - 229 IS - 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 A upon exposure to synchrotron X-rays. The crystals belong to the space group P4(1)2(1)2 (or P4(3)2(1)2) with unit cell dimensions of a = 38.02 A and c = 98.98 A. The presence of one molecule per asymmetric unit gives the unit cell volume per protein mass (Vm) of 1.99 A3/Da and the solvent fraction of 38.2% by volume. X-ray data have been collected to 2.0 A Bragg spacing from native crystals. SN - 0022-2836 UR - https://www.unboundmedicine.com/medline/citation/8421310/Crystallization_and_preliminary_X_ray_crystallographic_analysis_of_probable_amylase/protease_inhibitor_B_from_rice_seeds_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022-2836(83)71027-2 DB - PRIME DP - Unbound Medicine ER -