CRYSTALLIZATION AND PRELIMINARY-X-RAY STUDIES OF HUMAN ERYTHROCYTE ACYLPEPTIDE HYDROLASE

被引：18

作者：

FEESE, M

SCALONI, A

JONES, WM

MANNING, JM

REMINGTON, SJ

机构：

[1] UNIV OREGON,INST MOLEC BIOL,EUGENE,OR 97403

[2] UNIV OREGON,DEPT CHEM,EUGENE,OR 97403

[3] UNIV OREGON,DEPT PHYS,EUGENE,OR 97403

[4] ROCKEFELLER UNIV,NEW YORK,NY 10021

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1993年 / 233卷 / 03期

关键词：

CRYSTALLIZATION; X-RAY CRYSTALLOGRAPHY; HYDROLASE;

D O I：

10.1006/jmbi.1993.1531

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：

Crystals of acylpeptide hydrolase suitable for structure determination have been obtained. This enzyme removes the N-terminal formyl or acetyl group together with the first amino acid residue from N-terminal blocked peptides including bioactive peptides. One set of crystals, which diffract to 2.2 Å, are in space group P2 with cell dimensions a = 118.6 Å, b = 82.3 Å, c = 182.1 Å, β = 91.6°. The search for suitable heavy-atom derivatives is underway. © 1993 Academic Press Limited.

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页码：546 / 549

页数：4

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