1PS5

STRUCTURE OF THE MONOCLINIC C2 FORM OF HEN EGG-WHITE LYSOZYME AT 2.0 ANGSTROMS RESOLUTION

Summary for 1PS5

• Entry DOI: 10.2210/pdb1ps5/pdb
• Descriptor: Lysozyme C, SULFATE ION (3 entities in total)
• Functional Keywords: hydrolase, glycosidase
• Biological source: Gallus gallus (chicken)
• Cellular location: Secreted: P00698
• Total number of polymer chains: 1
• Total formula weight: 14523.29

Authors

Majeed, S.,Ofek, G.,Belachew, A.,Huang, C.,Zhou, T.,Kwong, P.D. (deposition date: 2003-06-20, release date: 2003-09-09, Last modification date: 2024-11-06)

Primary citation

Majeed, S.,Ofek, G.,Belachew, A.,Huang, C.,Zhou, T.,Kwong, P.D.
Enhancing Protein Crystallization through Precipitant Synergy
Structure, 11:1061-1070, 2003

PubMed Abstract: Suitable conditions for protein crystallization are commonly identified by screening combinations of independent factors that affect crystal formation. Because precipitating agents are prime determinants of crystallization, we investigated whether a systematic exploration of combinations of mechanistically distinct precipitants would enhance crystallization. A crystallization screen containing 64 precipitant mixtures was devised. Tests with ten HIV envelope-related proteins demonstrated that use of precipitant mixtures significantly enhanced both the probability of crystallization as well as the quality of optimized crystals. Tests with hen egg white lysozyme generated a novel C2 crystal from a salt/organic solvent mixture; structure solution at 2 A resolution revealed a lattice held together by both hydrophobic and electrostatic dyad interactions. The results indicate that mechanistically distinct precipitants can synergize, with precipitant combinations adding unique dimensions to protein crystallization.

PubMed: 12962625
DOI: 10.1016/S0969-2126(03)00185-0

Experimental method

X-RAY DIFFRACTION (2 Å)