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145 citations found for Huber,

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A low-temperature camera for single-crystal X-ray investigation between 28 and 350 K has been developed for a modified Weissenberg goniometer. Cooling is provided by a double-stage cryorefrigerator which is firmly attached to the low-temperature camera. Stranded copper cables ensure a flexible heat transfer between crystal and cold finger allowing a crystal rotation of 180°. Compared to the usual Weissenberg technique almost no further limitation is given on the accessible angular range of the scattered radiation.

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Acta Cryst. (1987). A43, C29
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A vacuum heating camera has been developed for extremely low background X-ray film work between room temperature and 2000 K. It can be used with modified conventional Weissenberg goniometers and with a specially designed focusing goniometer. The temperature control is maintained by a Pt/Pt-10% Rh thermocouple, a three-term proportional, integral and derivative (PID) controller and a programmable power supply. The accuracy in the absolute temperature setting is 10 K, the stability better than 1 K and the maximum thermal gradient over the crystal 7 K mm-1 at 1330 K. A small oxygen pressure can be applied, depending on the temperature, to control oxidation or reduction reactions of the sample.

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Acta Cryst. (2002). A58, c273
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The crystal structure of E. coli MoaB protein and a detailed comparison with the homologues MogA, Cnx1 G-domain and gephyrin are reported.

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Surface-residue mutagenesis and cocrystallization with Fab fragments, Fynomers or Xaperones were used to obtain the first high-resolution crystal structures of BACE2. These map the conformational space accessible to this potential drug target.


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Acta Cryst. (2011). A67, C674
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Acta Cryst. (2002). A58, c96
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Acta Cryst. (2006). A62, s71
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Acta Cryst. (2019). A75, e96
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Acetylene hydratase, a tungsten-containing hydroxylase that converts acetylene to acetaldehyde, has been purified and crystallized under anaerobic conditions.

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Bond-length and bond-angle parameters are derived from a statistical survey of X-ray structures of small compounds from the Cambridge Structural Database. The side chains of the common amino acids and the polypeptide backbone were represented by appropriate chemical fragments taken from the Database. Average bond lengths and bond angles are determined from the resulting samples and the sample standard deviations provide information regarding the expected variability of the average values which can be parametrized as force constants. These parameters are ideally suited for the refinement of protein structures determined by X-ray crystallography since they are derived from X-ray structures, are accurate to within the deviations from target values suggested for X-ray structure refinement and use force constants which directly reflect the variability or uncertainty of the average values. Tests of refinement of the structures of BPTI and phycocyanin demonstrate the integrity of the parameters and comparisons of equivalent refinements with XPLOR parameters show improvement in R-factors and geometry statistics.

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