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人红细胞酰基肽水解酶的结晶及初步X射线研究。

Crystallization and preliminary X-ray studies of human erythrocyte acylpeptide hydrolase.

作者信息

Feese M, Scaloni A, Jones W M, Manning J M, Remington S J

机构信息

Institute of Molecular Biology, University of Oregon, Eugene 97403.

出版信息

J Mol Biol. 1993 Oct 5;233(3):546-9. doi: 10.1006/jmbi.1993.1531.

DOI:10.1006/jmbi.1993.1531
PMID:8411161
Abstract

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 A, are in space group P2 with cell dimensions a = 118.6 A, b = 82.3 A, c = 182.1 A, beta = 91.6 degrees. The search for suitable heavy-atom derivatives is underway.

摘要

已获得适用于结构测定的酰基肽水解酶晶体。该酶能从包括生物活性肽在内的N端封闭肽中去除N端的甲酰基或乙酰基以及第一个氨基酸残基。一组能衍射至2.2埃的晶体,属于空间群P2,晶胞参数为a = 118.6埃,b = 82.3埃,c = 182.1埃,β = 91.6°。寻找合适的重原子衍生物的工作正在进行中。

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