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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Apr 1;65(Pt 4):389-91. doi: 10.1107/S1744309109008549. Epub 2009 Mar 25.

Crystallization and preliminary X-ray diffraction analysis of human seminal plasma protein PSP94.

Author information

1
Solid State Physics Division, Bhabha Atomic Research Centre, Trombay, Mumbai 400085, India. mukeshk@barc.gov.in

Abstract

The human seminal plasma protein PSP94 is a small protein of 94 residues that contains ten cysteines. Since its discovery about 25 years ago, several potential biological functions have been reported for this protein. Many PSP94 homologues have also been identified since then from various species, but no crystal structure has been determined to date. PSP94 has been purified from human seminal plasma and crystallized. These crystals diffracted to approximately 2.3 A resolution and belonged to space group P4(1)2(1)2, with unit-cell parameters a = 107.9, b = 107.9, c = 92.1 A. There are four molecules in the asymmetric unit. Structure solution by the heavy-atom method is currently in progress.

PMID:
19342788
PMCID:
PMC2664768
DOI:
10.1107/S1744309109008549
[Indexed for MEDLINE]
Free PMC Article

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