5gx1 | pdb_00005gx1

Luciferin-regenerating enzyme collected with serial synchrotron rotational crystallography with accumulated dose of 1.1 MGy (1st measurement)

spinqualitylabelsall models 5gx1, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5gx1 is a 1 chain structure with sequence from Photinus pyralis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: GOL, HG, MG, MPD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q95YI4_PHOPY Publication Abstract from PubMed Serial crystallography, in which single-shot diffraction images are collected, has great potential for protein microcrystallography. Although serial femtosecond crystallography (SFX) has been successfully demonstrated, limited beam time prevents its routine use. Inspired by SFX, serial synchrotron crystallography (SSX) has been investigated at synchrotron macromolecular crystallography beamlines. Unlike SFX, the longer exposure time of milliseconds to seconds commonly used in SSX causes radiation damage. However, in SSX, crystals can be rotated during the exposure, which can achieve efficient coverage of the reciprocal space. In this study, mercury single-wavelength anomalous diffraction (Hg-SAD) phasing of the luciferin regenerating enzyme (LRE) was performed using serial synchrotron rotation crystallography. The advantages of rotation and influence of dose on the data collected were evaluated. The results showed that sample rotation was effective for accurate data collection, and the optimum helical rotation step depended on multiple factors such as multiplicity and partiality of reflections, exposure time per rotation angle and the contribution from background scattering. For the LRE microcrystals, 0.25 degrees was the best rotation step for the achievable resolution limit, whereas a rotation step larger than or equal to 1 degrees was favorable for Hg-SAD phasing. Although an accumulated dose beyond 1.1 MGy caused specific damage at the Hg site, increases in resolution and anomalous signal were observed up to 3.4 MGy because of a higher signal-to-noise ratio. Development of a dose-limiting data collection strategy for serial synchrotron rotation crystallography.,Hasegawa K, Yamashita K, Murai T, Nuemket N, Hirata K, Ueno G, Ago H, Nakatsu T, Kumasaka T, Yamamoto M J Synchrotron Radiat. 2017 Jan 1;24(Pt 1):29-41. doi: 10.1107/S1600577516016362. , Epub 2017 Jan 1. PMID:28009544 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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