albumin - publications

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1. Int J Mol Sci. 2012;13(3):3782-800. Epub 2012 Mar 21.

Increasing the X-ray Diffraction Power of Protein Crystals by Dehydration: The
Case of Bovine Serum Albumin and a Survey of Literature Data.

Russo Krauss I, Sica F, Mattia CA, Merlino A.

Department of Chemical Sciences, University of Naples Federico II, Complesso
Universitario di Monte Sant'Angelo, Via Cinthia, Naples I-80126, Italy; E-Mails:
irene.russokrauss@unina.it (I.R.K.); filosica@unina.it (F.S.).

Serum albumin is one of the most widely studied proteins. It is the most abundant
protein in plasma with a typical concentration of 5 g/100 mL and the principal
transporter of fatty acids in plasma. While the crystal structures of human serum
albumin (HSA) free and in complex with fatty acids, hemin, and local anesthetics
have been characterized, no crystallographic models are available on bovine serum
albumin (BSA), presumably because of the poor diffraction power of existing
hexagonal BSA crystals. Here, the crystallization and diffraction data of a new
BSA crystal form, obtained by the hanging drop method using MPEG 5K as
precipitating agent, are presented. The crystals belong to space group C2, with
unit-cell parameters a = 216.45 Å, b = 44.72 Å, c = 140.18 Å, β = 114.5°.
Dehydration was found to increase the diffraction limit of BSA crystals from ~8 Å
to 3.2 Å, probably by improving the packing of protein molecules in the crystal
lattice. These results, together with a survey of more than 60 successful cases
of protein crystal dehydration, confirm that it can be a useful procedure to be
used in initial screening as a method of improving the diffraction limits of
existing crystals.

PMCID: PMC3317743
PMID: 22489183 [PubMed - in process]