1ps5

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spinqualitylabelsall models 1ps5, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Overview

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.

About this Structure

1PS5 is a Single protein structure of sequence from Gallus gallus with SO4 as ligand. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.

Reference

Enhancing protein crystallization through precipitant synergy., Majeed S, Ofek G, Belachew A, Huang CC, Zhou T, Kwong PD, Structure. 2003 Sep;11(9):1061-70. PMID:12962625

Page seeded by OCA on Wed Nov 21 00:04:31 2007