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


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.

SUBMITTER: Kumar M 

PROVIDER: S-EPMC2664768 | biostudies-literature | 2009 Apr

REPOSITORIES: biostudies-literature

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

Kumar Mukesh M   Jagtap Dhanashree D DD   Mahale Smita D SD   Prashar Vishal V   Kumar Ashwani A   Das Amit A   Bihani Subhash C SC   Ferrer Jean Luc JL   Hosur Madhusoodan V MV   Ramanadham M M  

Acta crystallographica. Section F, Structural biology and crystallization communications 20090325 Pt 4


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 spa  ...[more]

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