issue contents
February 2016 issue
IYCr crystallization series
Open access
An understanding of protein stability is essential for optimizing the expression, purification and crystallization of proteins. In this review, discussion will focus on factors affecting protein stability on a somewhat practical level, particularly from the view of a protein crystallographer.
This article reviews the role of mass transport in protein-crystallization experiments.
research communications
Open access
PA4991 is a FAD-dependent oxidoreductase from the pathogen P. aeruginosa that is essential for virulence and survival in the infected host. The structure of this enzyme, determined to 2.4 Å resolution, reveals that PA4991 belongs to the GR2 family of flavoenzymes.
PDB reference: FAD-dependent oxidoreductase PA4991, 5ez7
RNA helicases are essential key players in numerous cellular processes. Here, the crystal structure of the spliceosomal DEAH-box helicase Prp43 from C. thermophilum is reported and revealed to be capable of functionally replacing its yeast orthologue in spliceosomal disassembly assays.
Open access
The Spt16–SSRP1 heterodimer is a histone chaperone that plays an important role in regulating chromatin assembly. Here, a crystal structure of the N-terminal domain of human Spt16 is presented and it is shown that this domain may contribute to histone binding.
PDB reference: N-terminal domain of human Spt16, 5e5b
The crystal structure of the catalytic domain of MARK4 was determined and compared with those of other proteins belonging to the MARK/PAR-1 protein kinase family.
FleN from P. aeruginosa has been cloned, purified and crystallized.
The crystal structures of two conformations of M. tuberculosis EccB1 (states III and IV) are reported and are compared with two previously reported conformations (states I and II) in order to better understand the structure–function relationship of EccB1.
A chimeric fusion protein between the spindle-orientation protein LGN and the F-actin-binding protein afadin was generated and crystallized. The crystals belonged to space group P213 and diffracted to 3.0 Å resolution.
A new dehydration method to improve the diffraction resolution of protein crystals is reported.