Statistical analyses of the impact of X-ray damage effects on conformational heterogeneity in room temperature (277 K) and cryo-cooled (100 K) protein crystals
<p>These data are published in support of the manuscript "Evaluating the impact of X-ray damage on conformational heterogeneity in room temperature and cryo-cooled protein crystals" submitted to Acta Crystallographica section D, authors:</p> <p>Filip Yabukarski<sup>1,</sup><sup>#,</sup>*, Tzanko Doukov<sup>5</sup>, Daniel A Mokhtari<sup>1</sup>, Siyuan Du<sup>1</sup>, Daniel Herschlag<sup>1,2,3,4</sup><sup>,</sup>*</p> <p><sup>1</sup>Department of Biochemistry, <sup>2</sup>Department of Chemistry, <sup>3</sup>Department of Chemical Engineering, <sup>4</sup>Stanford ChEM-H, Stanford University, Stanford, California 94305, United States, <sup>5</sup>Stanford Synchrotron Radiation Light Source, SLAC National Accelerator Laboratory, Menlo Park, California 94025, United States.</p> <p># Current address: Bristol Myers Squibb, San Diego, California 92121, United States.</p> <p>* Correspondence: fyabukar@stanford.edu, herschla@stanford.edu</p>
ShareScore
36/100
Overall dataset sharing score
Score breakdown
These five areas show where the dataset supports — or may limit — practical reuse.
- Stewardship
- 8
- Harmonization
- 4
- Access
- 16
- Reuse readiness
- 8
- Engagement
- 0