PURIFICATION, CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC ANALYSIS OF PORCINE ALDOSE REDUCTASE

被引：8

作者：

ELKABBANI, O

NARAYANA, SVL

BABU, YS

MOORE, KM

FLYNN, TG

PETRASH, JM

WESTBROOK, EM

DELUCAS, LJ

BUGG, CE

机构：

[1] BIOCRYST INC,BIRMINGHAM,AL 35205

[2] QUEENS UNIV,DEPT BIOCHEM,KINGSTON K7L 3N6,ONTARIO,CANADA

[3] WASHINGTON UNIV,SCH MED,DEPT OPHTHALMOL & VISUAL SCI,ST LOUIS,MO 63110

[4] ARGONNE NATL LAB,BIOL ENVIRONM & MED RES,ARGONNE,IL 60439

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1991年 / 218卷 / 04期

关键词：

D O I：

10.1016/0022-2836(91)90257-7

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：

Large crystals of porcine aldose reductase have been grown from polyethylene glycol solutions. The crystals are triclinic, space-group P1, with a = 81.3 A ̊, b = 85.9 A ̊, c = 56.6 A ̊, α = 102.3 °, β = 103.3 ° and ψ = 79.0 °. The crystals grow within ten days to dimensions of 0.6 mm × 0.4 mm × 0.2 mm and diffract to at least 2.5 Å. There are four molecules in the unit cell related by a set of three mutually perpendicular non-crystallographic 2-fold axes. © 1991.

引用

页码：695 / 698

页数：4

共 18 条

[1]

BLUNDELL TL, 1976, PROTEIN CRYSTALLOGRA, P333

[2]

BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3

[3] ALDOSE REDUCTASE AND RHO-CRYSTALLIN BELONG TO THE SAME PROTEIN SUPERFAMILY AS ALDEHYDE REDUCTASE [J].