SASDCA6: SirA-like protein (DSY4693) from Desulfitobacterium hafniense, No...

Basic information

• Entry: Database: SASBDB / ID: SASDCA6

Sample

SirA-like protein (DSY4693) from Desulfitobacterium hafniense, Northeast Structural Genomics Consortium Target DhR2A

• Uncharacterized protein (protein), Desulfitobacterium hafniense (strain Y51)

• Function / homology: Selenium metabolism protein YedF / TusA-like domain / Sulfurtransferase TusA / TusA-like domain superfamily / DsrEFH-like / UPF0033 domain-containing protein
• Biological species: Desulfitobacterium hafniense (strain Y51) (bacteria)
• Citation: Journal: Biopolymers / Year: 2011; Title: Small angle X-ray scattering as a complementary tool for high-throughput structural studies.; Authors: Thomas D Grant / Joseph R Luft / Jennifer R Wolfley / Hiro Tsuruta / Anne Martel / Gaetano T Montelione / Edward H Snell / ; 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 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.

Models

• Model #1410: ; Type: dummy / Radius of dummy atoms: 1.25 A / Chi-square value: 1.723969; Search similar-shape structures of this assembly by Omokage search (details)
• Model #1414: ; Type: atomic / Radius of dummy atoms: 1.90 A / Chi-square value: 17.875984; Search similar-shape structures of this assembly by Omokage search (details)

Sample

• Sample: Name: SirA-like protein (DSY4693) from Desulfitobacterium hafniense, Northeast Structural Genomics Consortium Target DhR2A; Specimen concentration: 0.92-4.43
• Buffer: Name: 5 mM DTT 100 mM NaCl 10 mM Tris-HCl 0.02 % NaN3 / pH: 7.5

Entity #742

Type: protein / Description: Uncharacterized protein / Formula weight: 9.383 / Num. of mol.: 1 / Source: Desulfitobacterium hafniense (strain Y51) / References: UniProt: Q24NB0
Sequence:

MITIDALGQV CPIPVIRAKK ALAELGEAGG VVTVLVDNDI SRQNLQKMAE GMGYQAEYLE KDNGVIEVTI VAGEGCAVEL EHHHHHH

Experimental information

• Beam: Instrument name: Stanford Synchrotron Radiation Lightsource (SSRL) BL4-2; City: Stanford, CA / 国: USA / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.13 Å / Dist. spec. to detc.: 1.5 mm
• Detector: Name: Rayonix MX225-HE

Scan

Title: SirA-like protein (DSY4693) from Desulfitobacterium hafniense, Northeast Structural Genomics Consortium Target DhR2A
Measurement date: Feb 12, 2010 / Storage temperature: -80 °C / Cell temperature: 20 °C / Exposure time: 1 sec. / Number of frames: 20 / Unit: 1/A /

	Min	Max
Q	0.0196	0.3496

Distance distribution function P(R)

Sofotware P(R): GNOM 4.5a / Number of points: 354 /

	Min	Max
Q	0.02058	0.3496
P(R) point	1	354
R	0	53.19

Result

D max: 5.32 / Type of curve: single_conc /

	Experimental	Porod
MW	7.827 kDa	7.83 kDa
Volume	-	12.99 nm3

	P(R)	Guinier
Forward scattering, I0	438.3	434.9
Radius of gyration, Rg	1.572 nm	1.53 nm