Crystallography Research - X-Ray Crystals, Techniques, Analyses, Structures

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Analysis of solvent content and oligomeric states in protein crystals--does symmetry matter?

Chruszcz M, Potrzebowski W, Zimmerman MD, Grabowski M, Zheng H, Lasota P, Minor W

Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia 22908, USA.

A nonredundant set of 9081 protein crystal structures in the Protein Data Bank was used to examine the solvent content, the number of polypeptide chains, and the oligomeric states of proteins in crystals as a function of crystal symmetry (as classified by crystal systems and space groups). It was found that there is a correlation between solvent content and crystal symmetry. Surprisingly, proteins crystallizing in lower symmetry systems have lower solvent content compared to those crystallizing in higher symmetry systems. Nevertheless, there is no universal correlation between solvent content and preferences of macromolecules to crystallize in certain space groups. Crystal symmetry as a function of oligomeric state was examined, where trimers, tetramers, and hexamers were found to prefer to crystallize in systems where the oligomer symmetry could be incorporated in the crystal symmetry. Our analysis also shows that the frequency distribution within the enantiomorphous pairs of space groups does not differ significantly, in contrast to previous reports.

Published 24 March 2008 in Protein Sci, 17(4): 623-32.
Full-text of this article is available online (may require subscription).


Articles on Crystallography published 21 March 2008:

Small-angle X-ray scattering reveals the N-terminal domain organization of cardiac myosin binding protein C.   J Mol Biol, 377(4): 1186-99.

Myosin binding protein C (MyBP-C) is a multidomain accessory protein of striated muscle sarcomeres. Three domains at the N-terminus of MyBP-C (C1-m-C2) play a crucial role in maintaining and modulating actomyosin interactions. The cardiac isoform has an additional N-terminal domain (C0) that is postulated to provide a greater level of regulatory control in cardiac muscle. We have used small-angle X-ray scattering, ab initio shape restoration, and rigid-body modeling to determine the average ... [Abstract] [Full-text]


Articles on Crystallography published 13 March 2008:

Protein structure and hydration probed by SANS and osmotic stress.   Biophys J, 94(7): 2777-89.

Interactions governing protein folding, stability, recognition, and activity are mediated by hydration. Here, we use small-angle neutron scattering coupled with osmotic stress to investigate the hydration of two proteins, lysozyme and guanylate kinase (GK), in the presence of solutes. By taking advantage of the neutron contrast variation that occurs upon addition of these solutes, the number of protein-associated (solute-excluded) water molecules can be estimated from changes in both the ... [Abstract] [Full-text]


Articles on Crystallography published 3 March 2008:

Identification of cremains using X-ray diffraction spectroscopy and a comparison to trace element analysis.   Forensic Sci Int, 175(2): 218-26.

The ability to distinguish human cremains from filler materials can be important in a variety of situations, the most notorious recent example being the Tri-State Crematorium incident. However, the majority of the papers in the recent literature present methods that rely on trace or minor element analysis, usually followed by a statistical or variable cluster analysis, to determine attribution. This approach is inherently risky, as there is significant natural variation in the trace and minor ... [Abstract] [Full-text]


Articles on Crystallography published 25 February 2008:

The crystallographic study of left-handed Z-DNA d(CGCGCG)2 and thermine complexes crystallized at various temperatures and at various concentration of cations.   Biochem Biophys Res Commun, 368(2): 382-7.

In crystals of complexes of thermine and d(CGCGCG)2 molecules grown at 4, 10, and 20 degrees C, the numbers of thermine molecules connected to the DNA molecule were dependent on the temperature of the crystallization. Two molecules of thermine and one Mg2+ ion were connected to DNA molecule when thermine and d(CGCGCG)2 were co-crystallized at 4 and at 20 degrees C. When an increased concentration of magnesium and thermine molecules were co-crystallized with d(CGCGCG)2 molecules at 10 degrees C, ... [Abstract] [Full-text]


Articles on Crystallography published 13 February 2008:

2'-Methylseleno-modified oligoribonucleotides for X-ray crystallography synthesized by the ACE RNA solid-phase approach.   Nucleic Acids Res, 36(3): 970-83.

Site-specifically modified 2'-methylseleno RNA represents a valuable derivative for phasing of X-ray crystallographic data. Several successful applications in three-dimensional structure determination of nucleic acids, such as the Diels-Alder ribozyme, have relied on this modification. Here, we introduce synthetic routes to 2'-methylseleno phosphoramidite building blocks of all four standard nucleosides, adenosine, cytidine, guanosine and uridine, that are tailored for ... [Abstract] [Full-text]


Articles on Crystallography published 29 January 2008:

Membrane fusogenic activity of the Alzheimer's peptide A beta(1-42) demonstrated by small-angle neutron scattering.   J Mol Biol, 376(2): 393-404.

Amyloid-beta peptide (A beta) is considered a triggering agent of Alzheimer's disease. In relation to a therapeutic treatment of the disease, the interaction of A beta with the cell membrane has to be elucidated at the molecular level to understand its mechanism of action. In previous works, we had ascertained by neutron diffraction on stacked lipid multilayers that a toxic fragment of A beta is able to penetrate and perturb the lipid bilayer. Here, the influence of A beta(1-42), the most ... [Abstract] [Full-text]

Structural characterization of the active and inactive states of Src kinase in solution by small-angle X-ray scattering.   J Mol Biol, 376(2): 492-505.

Src kinase plays an important role in several signaling and regulation mechanisms in vivo. Enzymatic activity is tightly regulated through the phosphorylation and dephosphorylation of tyrosine 527, which is placed at the C-terminal tail. Here, we have addressed domain rearrangements involved in the regulation mechanism of Src kinase in solution using small-angle X-ray scattering. In the phosphorylated wild-type form of Src kinase corresponding to the inactive state of the protein, a single ... [Abstract] [Full-text]


Articles on Crystallography published 24 January 2008:

Asymmetry of the GroEL-GroES complex under physiological conditions as revealed by small-angle x-ray scattering.   Biophys J, 94(4): 1392-402.

Despite the well-known functional importance of GroEL-GroES complex formation during the chaperonin cycle, the stoichiometry of the complex has not been clarified. The complex can occur either as an asymmetric 1:1 GroEL-GroES complex or as a symmetric 1:2 GroEL-GroES complex, although it remains uncertain which type is predominant under physiological conditions. To resolve this question, we studied the structure of the GroEL-GroES complex under physiological conditions by small-angle x-ray ... [Abstract] [Full-text]


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Crystallography Research Today Archive:

Volume 1 (2005)
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Volume 4 (2008)
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