Preliminary XFEL data from spontaneously grown endo-1,4-β-xylanase crystals from Hypocrea virens

The enzymatic degradation of semi-cellulosic substrates has recently received immense attention. The enzyme endo-1,4-beta-xylanase is essential for the complete digestion of complex and heterogeneous hemicellulose. Here, the purification, crystallization and preliminary X-ray free-electron laser (XFEL) diffraction analysis of endo-1,4-beta-xylanase from the fungus Hypocrea virens (HviGH11) are reported. Codon-optimized HviGH11 was overexpressed in Escherichia coli and spontaneously crystallized after His-tag purification and concentration. Preliminary XFEL diffraction data were collected at the Pohang Accelerator Laboratory XFEL (PAL-XFEL). A total of 1021 images containing Bragg peaks were obtained and indexed. The HviGH11 crystals belonged to the orthorhombic space group P2(1)2(1)2(1) , with unit-cell parameters a = 43.80, b = 51.90, c = 94.90 angstrom. Using 956 diffraction patterns, the phasing problem was solved and an initial model structure of HviGH11 was obtained.

Automated summary

This study reports the purification, crystallization, and preliminary XFEL diffraction analysis of endo-1,4-beta-xylanase from the fungus Hypocrea virens. The enzyme was overexpressed in Escherichia coli and spontaneously crystallized after purification. Preliminary XFEL diffraction data were collected and solved the phasing problem to obtain the initial model structure of the enzyme.