Expression, purification and preliminary crystallographic studies of human hexokinasei

E. Sabini, C. Rosano, C. Capasso, M. Rizzi, M. Bolognesi, M. Bianchi, G. Serafini, E. Bartolucci, M. Magnani

Research output: Contribution to journalArticlepeer-review


Human hexokinase type I, one of the four isozymes consisting of a single polypeptide chain of about 100 kDa, has been cloned in the pET expression plasmid in a truncated form lacking a segment of 11 apolar amino acids at the N-terminus. The protein has been overexpressed in E.coli and purified to homogeneity. Truncated hexokinase I has been crystallized in the presence of glucose 6-phosphate and of the ATP analogue AMP-PNP. The crystals belong to the monoclinic space group P21, with unit cell constants: a = 84.2 Å, b = 177.7 Å, c = 88.2 Å, β = 90.8° and diffract to 3.0 A resolution.

Original languageEnglish
Pages (from-to)237-242
Number of pages6
JournalProtein and Peptide Letters
Issue number4
Publication statusPublished - 1998

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


Dive into the research topics of 'Expression, purification and preliminary crystallographic studies of human hexokinasei'. Together they form a unique fingerprint.

Cite this