Crystallization and preliminary X-ray crystallographic analysis of human nucleoside diphosphate kinase A

  • Kyeongsik Min
  • , Sun Young Kim
  • , Hyun Kyu Song
  • , Changsoo Chang
  • , Seung Je Cho
  • , Jinho Moon
  • , Jin Kuk Yang
  • , Jae Young Lee
  • , Kong Joo Lee
  • , Se Won Suh

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

Human nucleoside diphosphate kinase A catalyzes phosphoryl transfer and acts as a suppressor of metastasis. It has been crystallized using 2-methyl-2,4-pentanediol as a precipitant at 288 K. The crystal is monoclinic, belonging to the space group P21, with unit-cell parameters a = 74.21, b = 78.11, c = 82.29 Å, β = 101.33°. The asymmetric unit contains a homohexamer, with a corresponding crystal volume per protein mass (V(m)) of 2.27 Å3 Da-1 and a solvent content of 46%. Native X-ray data to 2.15 Å resolution have been collected using synchrotron X-rays.

Original languageEnglish
Pages (from-to)504-505
Number of pages2
JournalActa Crystallographica Section D: Biological Crystallography
Volume56
Issue number4
DOIs
StatePublished - 2000

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