Crystallization and preliminary X-ray crystallographic studies of human placental annexin IV

P S Freemont; H P Driessen; W Verbi; M J Crumpton

doi:10.1016/S0022-2836(05)80310-9

Crystallization and preliminary X-ray crystallographic studies of human placental annexin IV

J Mol Biol. 1990 Nov 20;216(2):219-21. doi: 10.1016/S0022-2836(05)80310-9.

Authors

P S Freemont¹, H P Driessen, W Verbi, M J Crumpton

Affiliation

¹ Protein Structure Laboratory, Imperial Cancer Research Fund Laboratories, London, U.K.

PMID: 2254922
DOI: 10.1016/S0022-2836(05)80310-9

Abstract

Human placental annexin IV, a member of the annexin family of calcium and phospholipid-binding proteins, has been crystallized by the vapour diffusion method in the presence of calcium, using polyethylene glycol 8000. The crystals are orthorhombic, space C222(1), cell dimensions a = 105.4 A, b = 115.7 A, c = 80.7 A and diffract to at least 2.5 A resolution on a synchrotron source.

MeSH terms

Binding Sites
Calcium / metabolism
Calcium-Binding Proteins / chemistry
Calcium-Binding Proteins / isolation & purification*
Calcium-Binding Proteins / metabolism
Crystallization
Female
Humans
Placenta / metabolism*
Pregnancy
Protein Conformation
X-Ray Diffraction

Substances

Calcium-Binding Proteins
Calcium