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December 2022 issue
Cover illustration: The structure of the hydrophobic leucinostatin derivative ZHAWOC6027 has been determined using host lattice display technology [Kiss et al. (2022), Acta Cryst. D78, 1439–1450]. Leucinostatins are highly toxic mycotoxins and the simplified derivative ZHAWOC6027, which exhibits antiprotozoal activity, has been studied. Two designed ankyrin-repeat proteins (DARPins) were used to immobilize ZHAWOC6027 in a host lattice, and the structure of the complex was determined by X-ray diffraction. The fusion construct EngBF_L1_E4_v1 is shown here as a molecular surface and coloured according to B factor, ZHAWOC6027 is shown as sticks with C atoms in magenta and symmetry-related EngBF (host lattice) molecules are shown as grey surfaces.
CCP4
The use of AlphaFold2 predictions for the detection and correction of sequence-register errors among protein structures determined using cryo-EM deposited in the Protein Data Bank is described.
research papers
T. Murakawa,
M. Suzuki,
K. Fukui,
T. Masuda,
M. Sugahara,
K. Tono,
T. Tanaka,
S. Iwata,
E. Nango,
T. Yano,
K. Tanizawa and
T. Okajima
Serial femtosecond X-ray crystallography was performed using a liquid-jet system on bacterial copper amine oxidase microcrystals anaerobically premixed with an amine substrate. The structure determined at 1.94 Å resolution revealed catalytic intermediates in two reduced forms, confirming that anaerobic conditions were well maintained throughout the measurements.
Host lattice display facilitated the crystallographic analysis of a hydrophobic peptide under aqueous conditions.
A new method is suggested for the calculation of maps of limited and eventually inhomogeneous resolution as an analytic function of all atomic parameters, including local resolution. Practical details of map calculation are discussed.
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