Crystallization and preliminary crystallographic analysis of human Ca 2+-loaded calbindin-D28k

Chang Zhang, Yuna Sun, Wei Wang, Yan Zhang, Ming Ma, Zhiyong Lou

Research output: Contribution to journalArticlepeer-review


Calbindin-D28k is a calcium-binding protein that belongs to the troponin C superfamily. It is expressed in many tissues, including brain, intestine, kidney and pancreas, and performs roles as both a calcium buffer and a calcium sensor and carries out diverse physiological functions of importance. In order to resolve the crystal structure of human calbindin-D28k and to gain a better understanding of its biological functions, recombinant human calbindin-D28k was crystallized at 291 K using PEG 3350 as precipitant and a 2.4 Å resolution X-ray data set was collected from a single flash-cooled crystal (100 K). The crystal belonged to space group C2, with unit-cell parameters a = 108.1, b = 28.2, c=70.6 Å, β=107.8°. The presence of one molecule per asymmetric unit is presumed, corresponding to a Matthews coefficient of 1.75 Å3 Da-1.

Original languageEnglish (US)
Pages (from-to)133-136
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number2
StatePublished - 2008
Externally publishedYes


  • Calbindin-D28k
  • Calcium-binding proteins

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics


Dive into the research topics of 'Crystallization and preliminary crystallographic analysis of human Ca 2+-loaded calbindin-D28k'. Together they form a unique fingerprint.

Cite this