PDBsum entry 5mjl

Hydrolase

PDB id: 5mjl

Contents

Protein chain

279 a.a.

Ligands

NHE

EPE

Metals

_CA

_CL

Waters ×322

PDB id:

5mjl

Name:

Hydrolase

Title:

Single-shot pink beam serial crystallography: proteinase k

Structure:

Proteinase k. Chain: a. Synonym: endopeptidase k,tritirachium alkaline proteinase. Engineered: yes

Source:

Engyodontium album. Organism_taxid: 37998. Gene: prok. Expressed in: engyodontium album. Expression_system_taxid: 37998

Resolution:

2.21Å R-factor: 0.157 R-free: 0.195

Authors:

A.Meents,D.Oberthuer,J.Lieske,V.Srajer

Key ref:

A.Meents et al. (2017). Pink-beam serial crystallography. Nat Commun, 8, 1281. PubMed id: 29097720

Date:

01-Dec-16 Release date: 15-Nov-17

Protein chain

P06873  (PRTK_PARAQ) -  Proteinase K from Parengyodontium album

Seq: 384 a.a.

Struc: 279 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.3.4.21.64 - peptidase K.
• Reaction: Hydrolysis of keratin and of other proteins, with subtilisin-like specificity. Hydrolyzes peptides amides.

Nat Commun 8:1281 (2017)

PubMed id: 29097720

Pink-beam serial crystallography.

A.Meents, M.O.Wiedorn, V.Srajer, R.Henning, I.Sarrou, J.Bergtholdt, M.Barthelmess, P.Y.A.Reinke, D.Dierksmeyer, A.Tolstikova, S.Schaible, M.Messerschmidt, C.M.Ogata, D.J.Kissick, M.H.Taft, D.J.Manstein, J.Lieske, D.Oberthuer, R.F.Fischetti, H.N.Chapman.

ABSTRACT

Serial X-ray crystallography allows macromolecular structure determination at both X-ray free electron lasers (XFELs) and, more recently, synchrotron sources. The time resolution for serial synchrotron crystallography experiments has been limited to millisecond timescales with monochromatic beams. The polychromatic, "pink", beam provides a more than two orders of magnitude increased photon flux and hence allows accessing much shorter timescales in diffraction experiments at synchrotron sources. Here we report the structure determination of two different protein samples by merging pink-beam diffraction patterns from many crystals, each collected with a single 100 ps X-ray pulse exposure per crystal using a setup optimized for very low scattering background. In contrast to experiments with monochromatic radiation, data from only 50 crystals were required to obtain complete datasets. The high quality of the diffraction data highlights the potential of this method for studying irreversible reactions at sub-microsecond timescales using high-brightness X-ray facilities.