ArticleThe journal of physical chemistry. B2007
Crystal polymorphism of protein GB1 examined by solid-state NMR spectroscopy and X-ray diffraction.
Article in The journal of physical chemistry. B, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.
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Who cites it
73 citing papers in PubMed, 135 citations in OpenAlex.
- Evaluating the rate of hindered rotation of asparagine and glutamine side-chain amides in proteins using 'chemical-shift-averaged' ZZ-exchange NMR spectroscopy.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2026Article
- Genetically Encoded Pentafluorophenylalanine Enables Quantitative Probing of Local Protein Malleability by 19F NMR.Journal of the American Chemical Society · 2026Article
- Single crystal sapphire spacers for in situ angle sensing and rotor stability diagnostics in MAS NMR.Solid state nuclear magnetic resonance · 2026Article
- Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes.Nature chemistry · 2026Article
- DNP enhanced solid-state NMR of lattice-like microcrystalline protein assemblies facilitated by co-assembly with dinitroxide-tagged proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2026Article
- Carbon-13 Centerband-Only Detection of EXchange with Dynamic Nuclear Polarization.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026Article
- Measuring long-range contacts in a fully protonated protein at 105 kHz magic angle spinning.Journal of biomolecular NMR · 2025Article
- Visualize Transient Water-Mediated Hydrogen Bonds Facilitating the Formation of Enzymatic Near-Attack Conformers.JACS Au · 2025Article
- Rigid and stable nitroxide spin label for high-resolution distance measurements on proteins by DEER experiments.Magnetic resonance letters · 2025Article
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- Inter-residue through-space scalarMagnetic resonance (Gottingen, Germany) · 2025Article
- IntegratingJournal of the American Chemical Society · 2024Article
- Rapid Quantification of Protein Secondary Structure Composition from a Single Unassigned 1DJournal of the American Chemical Society · 2024Article
- Probing effects of site-specific aspartic acid isomerization on structure and stability of GB1 through chemical protein synthesis.Protein science : a publication of the Protein Society · 2024Article
- Modeling of Cu(II)-based protein spin labels using rotamer libraries.Physical chemistry chemical physics : PCCP · 2024Article
- Enlarging the scenario of site directedScientific reports · 2023Article
- 3D-Printable centrifugal devices for biomolecular solid state NMR rotors.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2023Article
- New experimental evidence for pervasive dynamics in proteins.Protein science : a publication of the Protein Society · 2023Article
- Ultrafast Magic Angle Spinning Solid-State NMR Spectroscopy: Advances in Methodology and Applications.Chemical reviews · 2023Review
- Molecular elucidation of drug-induced abnormal assemblies of the hepatitis B virus capsid protein by solid-state NMR.Nature communications · 2023Article
13 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
The study of micro- or nanocrystalline proteins by magic-angle spinning (MAS) solid-state NMR (SSNMR) gives atomic-resolution insight into structure in cases when single crystals cannot be obtained for diffraction studies. Subtle differences in the local chemical environment around the protein, including the characteristics of the cosolvent and the buffer, determine whether a protein will form single crystals. The impact of these small changes in formulation is also evident in the SSNMR spectra; however, the changes lead only to correspondingly subtle changes in the spectra. Here, we demonstrate that several formulations of GB1 microcrystals yield very high quality SSNMR spectra, although only a subset of conditions enable growth of single crystals. We have characterized these polymorphs by X-ray powder diffraction and assigned the SSNMR spectra. Assignments of the 13C and 15N SSNMR chemical shifts confirm that the backbone structure is conserved, indicative of a common protein fold, but side chain chemical shifts are changed on the surface of the protein, in a manner dependent upon crystal packing and electrostatic interactions with salt in the mother liquor. Our results demonstrate the ability of SSNMR to reveal minor structural differences among crystal polymorphs. This ability has potential practical utility for studying the formulation chemistry of industrial and therapeutic proteins, as well as for deriving fundamental insights into the phenomenon of single-crystal growth.
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