Crystallization of a small fragment of an aminoacyl tRNA synthetase

Christin A. Frederick, Andrew H.J. Wang, Alexander Rich, Lynne Regan, Paul Schimmel

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)

Abstract

Single crystals of an amino-terminal fragment of Escherichia coli alanine tRNA synthetase have been prepared by the vapor diffusion method. The fragment extends to amino acid residue 368 and catalyzes the synthesis of alanyl adenylate. The crystals grow in the presence of alanine as rhombic plates in space group P212121 and with unit cell dimensions of a = 67.9 A ̊, b = 98.5 A ̊ and c = 123.6 A ̊ (1 Å = 0.1 nm). They diffract to better than 3 Å resolution.

Original languageEnglish
Pages (from-to)521-522
Number of pages2
JournalJournal of Molecular Biology
Volume203
Issue number2
DOIs
Publication statusPublished - Sep 20 1988
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Fingerprint

Dive into the research topics of 'Crystallization of a small fragment of an aminoacyl tRNA synthetase'. Together they form a unique fingerprint.

Cite this