CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF THE COMMON-TYPE ACYLPHOSPHATASE

被引：5
作者：
THUNNISSEN, MMGM
AGANGO, EG
TADDEI, N
LIGURI, G
CECCHI, C
PIERI, A
RAMPONI, G
NORDLUND, P
机构：
[1] STOCKHOLM UNIV,DEPT BIOL MOLEC,S-10691 STOCKHOLM,SWEDEN
[2] UNIV FLORENCE,DEPT BIOCHEM SCI,FLORENCE,ITALY
来源：
FEBS LETTERS | 1995年 / 364卷 / 03期
关键词：
ACYLPHOSPHATASE; PROTEIN CRYSTALLIZATION; X-RAY DIFFRACTION; STRUCTURE DETERMINATION;
D O I：
10.1016/0014-5793(95)00363-E
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：
Single crystals of a 'common-type' acylphosphatase from bovine testis have been grown, Crystals belong to space group C2 and have cell dimensions a = 64.6 Angstrom, b = 36.5 Angstrom, c = 45.2 Angstrom and beta = 104.8 and contain one monomer per asymmetric unit, The crystals diffract better than 2.0 Angstrom resolution and are well suited for an X-ray structure determination.
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页码：243 / 244
页数：2
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