A simple vapor-diffusion method enables protein crystallization inside the HARE serial crystallography chip.

ABSTRACT: Fixed-target serial crystallography has become an important method for the study of protein structure and dynamics at synchrotrons and X-ray free-electron lasers. However, sample homogeneity, consumption and the physical stress on samples remain major challenges for these high-throughput experiments, which depend on high-quality protein microcrystals. The batch crystallization procedures that are typically applied require time- and sample-intensive screening and optimization. Here, a simple protein crystallization method inside the features of the HARE serial crystallography chips is reported that circumvents batch crystallization and allows the direct transfer of canonical vapor-diffusion conditions to in-chip crystallization. Based on conventional hanging-drop vapor-diffusion experiments

SUBMITTER: Norton-Baker B 

PROVIDER: S-EPMC8171066 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature