4B49
1.15 A Structure of Lysozyme Crystallized without 2-methyl-2,4- pentanediol
Summary for 4B49
Entry DOI | 10.2210/pdb4b49/pdb |
Descriptor | LYSOZYME C, CHLORIDE ION, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total) |
Functional Keywords | hydrolase, chirality |
Biological source | GALLUS GALLUS (CHICKEN) |
Total number of polymer chains | 1 |
Total formula weight | 14559.66 |
Authors | Jakoncic, J.,Berger, J.,Stauber, M.,Axelbaum, A.,Asherie, N. (deposition date: 2012-07-28, release date: 2012-08-22, Last modification date: 2024-10-09) |
Primary citation | Stauber, M.,Jakoncic, J.,Berger, J.,Karp, J.M.,Axelbaum, A.,Sastow, D.,Buldyrev, S.V.,Hrnjez, B.J.,Asherie, N. Crystallization of Lysozyme with (R)-, (S)- and (Rs)-2-Methyl-2,4-Pentanediol Acta Crystallogr.,Sect.D, 71:427-, 2015 Cited by PubMed Abstract: Chiral control of crystallization has ample precedent in the small-molecule world, but relatively little is known about the role of chirality in protein crystallization. In this study, lysozyme was crystallized in the presence of the chiral additive 2-methyl-2,4-pentanediol (MPD) separately using the R and S enantiomers as well as with a racemic RS mixture. Crystals grown with (R)-MPD had the most order and produced the highest resolution protein structures. This result is consistent with the observation that in the crystals grown with (R)-MPD and (RS)-MPD the crystal contacts are made by (R)-MPD, demonstrating that there is preferential interaction between lysozyme and this enantiomer. These findings suggest that chiral interactions are important in protein crystallization. PubMed: 25760593DOI: 10.1107/S1399004714025061 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.15 Å) |
Structure validation
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