Crystallization and preliminary X-ray diffraction data for the cyclic AMP receptor protein of Escherichia coli

David B. McKay, Michael G. Fried

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

The cyclic AMP receptor protein (CRP) of Escherichia coli has been crystallized. The crystals are orthorhombic, space group P212121, a = 46.5 A ̊, b = 97.1 Å, c = 105.4 A ̊, with one dimeric CRP molecule per asymmetric unit.

Original languageEnglish
Pages (from-to)95-96
Number of pages2
JournalJournal of Molecular Biology
Volume139
Issue number1
DOIs
StatePublished - May 5 1980

Bibliographical note

Funding Information:
was supported by U.S. Public Health Service predoctoral kainee-D. B. M. was supported by American Cancer Society postdoctoral Facilities support was pro\rided by U.S. Public Health Service, M. Crot,hers and GM-22778 to T. A. Steitz.

Funding Information:
One of’ us (M. 0. E’.) ship no. GM-07723-05; fellowship no. PF-1562. grants GM-21966 to D.

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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