当前位置： SCI文献检索 > JOURNAL OF STRUCTURAL BIOLOGY期刊下所有文献 > Purification, crystallization, and preliminary X-ray diffraction analysis of the Tricorn protease hexamer from Thermoplasma acidophilum.

Purification, crystallization, and preliminary X-ray diffraction analysis of the Tricorn protease hexamer from Thermoplasma acidophilum.

Abstract：

:Tricorn protease from Thermoplasma acidophilum is a hexameric enzyme; in vivo the hexamers assemble further to form large icosahedral capsids of 14.6 MDa. Recombinant Tricorn protease was purified as an enzymatically active hexamer of 0.72 MDa that formed crystals of octahedral morphology under low-ionic-strength conditions. These crystals belong to space group C2 with unit cell dimensions a = 307.5 A, b = 163.2 A, c = 220.9 A, beta = 105.5 degrees and diffract to 2.2-A resolution using high-brilliance synchrotron radiation. Based on analysis of the self-rotation function and the presence of a pseudo-origin peak in the native Patterson map, a packing model was derived for the complex, comprising 1.5 hexamers per asymmetric unit with a solvent content of 43%. Due to the ninefold noncrystallographic symmetry the Tricorn crystals represent an interesting case for phasing X-ray crystallographic data by electron microscopic phase information.

journal_name

J Struct Biol

journal_title

Journal of structural biology

authors

Bosch J,Tamura T,Bourenkov G,Baumeister W,Essen LO

doi

10.1006/jsbi.2001.4360

keywords:

subject

Has Abstract

pub_date

2001-04-01 00:00:00

pages

83-7

issue

1

eissn

1047-8477

issn

1095-8657

pii

S1047-8477(01)94360-6

journal_volume

134

pub_type

杂志文章

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