issue contents

ISSN: 2053-230X

February 2016 issue

Highlighted illustration

Cover illustration: Microtubule affinity-regulating kinase 4 catalytic domain in complex with a pyrazolopyrimidine inhibitor (Sack et al., p. 129).

IYCr crystallization series

Acta Cryst. (2016). F72, 72-95
doi: 10.1107/S2053230X15024619
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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.

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This article reviews the role of mass transport in protein-crystallization experiments.

research communications

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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.

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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.

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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.

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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.

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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.

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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.

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A new dehydration method to improve the diffraction resolution of protein crystals is reported.
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