CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC ANALYSIS OF CARBOXYPEPTIDASE-G2 FROM PSEUDOMONAS-SP STRAIN RS-16

被引：9

作者：

LLOYD, LF ^{[1
]}

COLLYER, CA ^{[1
]}

SHERWOOD, RF ^{[1
]}

机构：

[1] PUBL HLTH LAB SERV,CTR APPL MICROBIOL & RES,DIV BIOTECHNOL,SALISBURY SP4 0JG,WILTS,ENGLAND

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1991年 / 220卷 / 01期

关键词：

CRYSTALLIZATION; CARBOXYPEPTIDASE-G2 FROM PSEUDOMONAS-SP STRAIN RS-16;

D O I：

10.1016/0022-2836(91)90377-I

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：

Carboxypeptidase G2 a zinc metalloenzyme isolated from Pseudomonas sp. strain RS-16, which catalyses the hydrolytic cleavage of reduced and non-reduced folates to pteroates and l-glutamate, has been crystallized from polyethylene glycol (average Mr 4000) by vapour diffusion. The crystal symmetry is monoclinic C2, with unit cell dimensions a = 206 A ̊, b = 82 A ̊, c = 116 A ̊ and β = 118 °. The molecular mass and volume of the unit cell suggest that there are two dimers of the enzyme in the asymmetric unit. The crystals diffract to at least 3·0 Å and are suitable for X-ray structure analysis. © 1991.

引用

页码：17 / 18

页数：2

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