Crystallization and preliminary crystallographic studies of trichomaglin, a novel ribosome-inactivating protein

J Wu; J H Gan; Z X Xia

doi:10.1107/s0907444900010660

Crystallization and preliminary crystallographic studies of trichomaglin, a novel ribosome-inactivating protein

Acta Crystallogr D Biol Crystallogr. 2000 Nov;56(Pt 11):1466-7. doi: 10.1107/s0907444900010660.

Authors

J Wu¹, J H Gan, Z X Xia

Affiliation

¹ State Key Laboratory of Bio-organic and Natural Products Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 200032, People's Republic of China.

PMID: 11053854
DOI: 10.1107/s0907444900010660

Abstract

Trichomaglin, a novel ribosome-inactivating protein, has been crystallized in two crystal forms using the hanging-drop vapour-diffusion method. The form A and form B crystals belong to the orthorhombic space group P2(1)2(1)2(1) and the hexagonal space group P6(1) (or P6(5)), respectively. X-ray data have been collected to 3.3 and 2.2 A resolution for the form A and B crystals, respectively.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Crystallization
Crystallography, X-Ray
N-Glycosyl Hydrolases / chemistry*
N-Glycosyl Hydrolases / pharmacology
Plant Proteins*
Ribosome Inactivating Proteins, Type 1
Ribosomes / drug effects*

Substances

Plant Proteins
Ribosome Inactivating Proteins, Type 1
N-Glycosyl Hydrolases
trichomaglin