PDBsum entry 4woc

Hydrolase

PDB id: 4woc

Contents

Protein chain

279 a.a.

Ligands

SO4 ×2

Waters ×346

PDB id:

4woc

Name:

Hydrolase

Title:

Proteinase-k post-surface acoustic waves

Structure:

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

Source:

Parengyodontium album. Tritirachium album. Organism_taxid: 37998. Gene: prok. Expressed in: tritirachium. Expression_system_taxid: 1001993

Resolution:

1.60Å R-factor: 0.176 R-free: 0.207

Authors:

J.B.French

Key ref:

F.Guo et al. (2015). Precise Manipulation and Patterning of Protein Crystals for Macromolecular Crystallography Using Surface Acoustic Waves. Small, 11, 2733-2737. PubMed id: 25641793 DOI: 10.1002/smll.201403262

Date:

15-Oct-14 Release date: 18-Feb-15

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.

DOI no: 10.1002/smll.201403262

Small 11:2733-2737 (2015)

PubMed id: 25641793

Precise Manipulation and Patterning of Protein Crystals for Macromolecular Crystallography Using Surface Acoustic Waves.

F.Guo, W.Zhou, P.Li, Z.Mao, N.H.Yennawar, J.B.French, T.J.Huang.

ABSTRACT

Advances in modern X-ray sources and detector technology have made it possible for crystallographers to collect usable data on crystals of only a few micrometers or less in size. Despite these developments, sample handling techniques have significantly lagged behind and often prevent the full realization of current beamline capabilities. In order to address this shortcoming, a surface acoustic wave-based method for manipulating and patterning crystals is developed. This method, which does not damage the fragile protein crystals, can precisely manipulate and pattern micrometer and submicrometer-sized crystals for data collection and screening. The technique is robust, inexpensive, and easy to implement. This method not only promises to significantly increase efficiency and throughput of both conventional and serial crystallography experiments, but will also make it possible to collect data on samples that were previously intractable.