Thomas D Grant / Joseph R Luft / Jennifer R Wolfley / Hiro Tsuruta / Anne Martel / Gaetano T Montelione / Edward H Snell /
PubMed Abstract
Structural crystallography and nuclear magnetic resonance (NMR) spectroscopy are the predominant techniques for understanding the biological world on a molecular level. Crystallography is constrained ...Structural crystallography and nuclear magnetic resonance (NMR) spectroscopy are the predominant techniques for understanding the biological world on a molecular level. Crystallography is constrained by the ability to form a crystal that diffracts well and NMR is constrained to smaller proteins. Although powerful techniques, they leave many soluble, purified structurally uncharacterized protein samples. Small angle X-ray scattering (SAXS) is a solution technique that provides data on the size and multiple conformations of a sample, and can be used to reconstruct a low-resolution molecular envelope of a macromolecule. In this study, SAXS has been used in a high-throughput manner on a subset of 28 proteins, where structural information is available from crystallographic and/or NMR techniques. These crystallographic and NMR structures were used to validate the accuracy of molecular envelopes reconstructed from SAXS data on a statistical level, to compare and highlight complementary structural information that SAXS provides, and to leverage biological information derived by crystallographers and spectroscopists from their structures. All the ab initio molecular envelopes calculated from the SAXS data agree well with the available structural information. SAXS is a powerful albeit low-resolution technique that can provide additional structural information in a high-throughput and complementary manner to improve the functional interpretation of high-resolution structures.
SASDC96: N-terminal domain of Diguanylate cyclase with PAS/PAC sensor (Maqu_2914) from Marinobacter aquaeolei, Northeast Structural Genomics Consortium Target MqR66C Method: SAXS/SANS
SASDCA6: SirA-like protein (DSY4693) from Desulfitobacterium hafniense, Northeast Structural Genomics Consortium Target DhR2A Method: SAXS/SANS
SASDCB6: Nmul_A1745 protein from Nitrosospira multiformis, Northeast Structural Genomics Consortium Target NmR72 Method: SAXS/SANS
SASDCC6: Sensory box domain of the sensory-box/GGDEF protein SO_1695 from Shewanella oneidensis, Northeast Structural Genomics Consortium Target SoR288B Method: SAXS/SANS
SASDCD6: MucBP domain of the adhesion protein PEPE_0118 from Pediococcus pentosaceus. Northeast Structural Genomics Consortium target id PtR41A Method: SAXS/SANS
SASDCE6: PAS domain of the protein CPS_1291 from Colwellia psychrerythraea. Northeast Structural Genomics Consortium target id CsR222B Method: SAXS/SANS
SASDCF6: HIT family hydrolase protein from Vibrio fischeri. Northeast Structural Genomics Consortium target id VfR176 Method: SAXS/SANS
SASDCG6: EAL/GGDEF domain protein from M. capsulatus, Northeast Structural Genomics Consortium Target McR174C Method: SAXS/SANS
SASDCH6: GGDEF domain from Marinobacter aquaeolei diguanylate cyclase complexed with c-di-GMP - Northeast Structural Genomics Consortium Target MqR89a Method: SAXS/SANS
SASDCJ6: MmoQ Response regulator (fragment 20-298) from Methylococcus capsulatus str. Bath, Northeast Structural Genomics Consortium Target McR175G Method: SAXS/SANS
SASDCK6: Sheath tail protein (DSY3957) from Desulfitobacterium hafniense, Northeast Structural Genomics Consortium Target DhR18 Method: SAXS/SANS
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