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4B4J

1.25 A Structure of Lysozyme Crystallized with (RS)-2-methyl-2,4- pentanediol

Summary for 4B4J
Entry DOI10.2210/pdb4b4j/pdb
Related4B49 4B4E 4B4I
DescriptorLYSOZYME C, CHLORIDE ION, (4R)-2-METHYLPENTANE-2,4-DIOL, ... (4 entities in total)
Functional Keywordshydrolase, chirality
Biological sourceGALLUS GALLUS (CHICKEN)
Total number of polymer chains1
Total formula weight14638.41
Authors
Jakoncic, J.,Berger, J.,Stauber, M.,Axelbaum, A.,Asherie, N. (deposition date: 2012-07-30, release date: 2012-08-22, Last modification date: 2024-11-06)
Primary citationStauber, 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: 25760593
DOI: 10.1107/S1399004714025061
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.25 Å)
Structure validation

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