Crystallization and preliminary X-ray crystallographic studies of ribonuclease LE from Lycopersicon esculentum

被引：0
|
作者：
Tanaka, N
Arai, J
Inokuchi, N
Koyama, T
Ohgi, K
Irie, M
Nakamura, KT
机构：
[1] Showa Univ, Sch Pharmaceut Sci, Tokyo 1428555, Japan
[2] Hoshi Coll Pharm, Tokyo 1428501, Japan
[3] Nihon Univ, Coll Pharm, Chiba 2740063, Japan
来源：
PROTEIN AND PEPTIDE LETTERS | 1999年 / 6卷 / 06期
关键词：
D O I：
暂无
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The ribonuclease LE, a plant ribonuclease from Lycopersicon esculentum, has been crystallized by the hanging-drop vapour diffusion method using polyethylene glycol 1,540 as the precipitating agent. The crystals belong to an orthorhombic space group P2(1)2(1)2(1) with cell dimensions of a = 74.10 Angstrom, b = 78.72 Angstrom, and c = 33.00 Angstrom. There is one molecule per asymmetric unit. The crystals diffract to at least 2.0 Angstrom resolution and are suitable for X-ray structure analysis at high resolution.
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页码：407 / 410
页数：4
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