Crystallization and preliminary X-ray crystallographic analysis of deoxycytidylate hydroxymethylase from bacteriophage T4

Se Hui Sohn, Hyun Kyu Song, Kyeongsik Min, Seung Je Cho, Jinho Moon, Jae Young Lee, Hyung Jun Ahn, Changsoo Chang, Hie Joon Kim, Se Won Suh

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Deoxycytidylate hydroxymethylase from bacteriophage T4 is a homodimeric enzyme in which each polypeptide chain consists of 246 amino-acid residues. It has been crystallized in the presence of its substrate, deoxycytidine monophosphate, at room temperature using sodium citrate as precipitant. The crystals are monoclinic, belonging to space group C2, with unit-cell parameters a = 174.22, b = 53.12, c = 75.17 Å, β = 115.29°. The asymmetric unit contains one homodimer, with a corresponding V(m) of 2.65 Å3 Da-1 and solvent content of 54%. Native diffraction data to 1.6 Å resolution have been collected from two crystals using synchrotron radiation.

Original languageEnglish
Pages (from-to)1061-1063
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume55
Issue number5
DOIs
Publication statusPublished - 1999 May

ASJC Scopus subject areas

  • Structural Biology

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