[English] 日本語
![](img/lk-miru.gif)
- SASDCF6: HIT family hydrolase protein from Vibrio fischeri. Northeast Stru... -
+
Open data
-
Basic information
Entry | Database: SASBDB / ID: SASDCF6 |
---|---|
![]() | HIT family hydrolase protein from Vibrio fischeri. Northeast Structural Genomics Consortium target id VfR176
|
Function / homology | Histidine triad hydrolase, Hint-type / HIT domain / HIT domain profile. / HIT-like domain / HIT-like superfamily / ![]() ![]() |
Biological species | ![]() ![]() |
![]() | ![]() 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 ...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. |
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-Data source
SASBDB page | ![]() |
---|
-Related structure data
Related structure data | C: citing same article ( |
---|---|
Similar structure data |
-
External links
Related items in Molecule of the Month |
---|
-Models
Model #1428 | ![]() Type: atomic / Radius of dummy atoms: 1.90 A / Chi-square value: 3.908529 ![]() |
---|---|
Model #1430 | ![]() Type: dummy / Radius of dummy atoms: 2.00 A / Chi-square value: 2.396304 ![]() |
-
Sample
![]() | Name: HIT family hydrolase protein from Vibrio fischeri. Northeast Structural Genomics Consortium target id VfR176 Specimen concentration: 2.08-6.26 |
---|---|
Buffer | Name: 5 mM DTT 100 mM NaCl 10 mM Tris-HCl 0.02 % NaN3 / pH: 7.5 |
Entity #750 | Type: protein / Description: HIT family hydrolase / Formula weight: 16.995 / Num. of mol.: 2 / Source: Vibrio fischeri (strain ATCC 700601 / ES114) / References: UniProt: Q5E3V1 Sequence: MAFQLHPRLQ QDCIVLGNLP LCKVLLIKED IGPWLILVPR IEELKEIHHM TDEQQIQFIK ESSAVAQLLE DNFSPDKINI GALGNLVPQL HIHHIARFTT DVAWPGPVWG NTTGVIRAQS SQTQLVDLLR DKLSNISGFK RLEHHHHHH |
-Experimental information
Beam | Instrument name: Stanford Synchrotron Radiation Lightsource (SSRL) BL4-2 City: Stanford, CA / 国: USA ![]() ![]() | ||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Detector | Name: Rayonix MX225-HE | ||||||||||||||||||
Scan | Measurement date: Feb 12, 2010 / Storage temperature: -80 °C / Cell temperature: 20 °C / Exposure time: 1 sec. / Number of frames: 20 / Unit: 1/A /
| ||||||||||||||||||
Distance distribution function P(R) |
| ||||||||||||||||||
Result |
|